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  • 1995-1999  (304)
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  • Life Sciences (general)
  • 1
    Electronic Resource
    Electronic Resource
    Umwelt-Mikrobiologie. Berlin, Heidelberg, New York, London, Paris, Tokyo, Hong Kong: Springer Verlag, 1998, 252 pages, 106 figures, 7 tables; DM 49.80. ISBN 3-437-35008-0 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 241-241 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180307
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  • 2
    Electronic Resource
    Electronic Resource
    Protection of biotechnological matter under European and German law. A handbook for applicants (first edition). Weinheim, New York, Basel, Cambridge, Tokyo: VCH Verlagsgesellschaft mbH, 1997, XVIII + 450 pages; DM 178.00. ISBN 3-527-28781-7 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 242-242 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180308
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  • 3
    Electronic Resource
    Electronic Resource
    Handbuch des Umweltschutzes und der Umweltschutztechnik. Additiver Umweltschutz: Behandlung von Abluft und Abgasen (Volume 3). Berlin, Heidelberg, New York, Barcelona, Budapest, Hong Kong, London, Milan, Paris, Santa Clara, Singapore, Tokyo: Springer Verlag XXVIII + 680 pages, 374 figures, 47 tables; DM 118.00 ISBN 3-540-58060-3 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 265-266 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180311
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  • 4
    Electronic Resource
    Electronic Resource
    The effect of chemical treatment of stainless steel wire surfaces on Zymomonas mobilis cell attachment and product synthesis (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 255-265 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The attachment, growth and product synthesis of non-flocculating Zymomonas mobilis cell, fixed in stainless steel wire spheres (WS), were investigated. The carrier surface was activated by treatment with titanium (IV) chloride (TiCl4) and γ-aminopropyltriethoxysilane (AS) in an attempt to raise the efficiency in the immobilization of the cells. System productivity for ethanol and levan production, using cells immobilized on a modified stainless steel in the batch fermentation of a sucrose medium, rose as a result of increased biomass compared to the productivity of cells fixed on untreated (control) metal surfaces. Stabilized ethanol synthesis was demonstrated in the course of four cycles (each cycle 48 h) of repeated fermentations with a stainless steel carrier treated with AS, and three cycles when TiCl4 was used. Levan synthesis decreased after three cycles with cells immobilized on a silanized surface. System productivity for ethanol and levan production after the fourth cycle in experiments with TiCl4-activated, silanized and unmodified carriers were Qeth = 1.01, 1.06 and 0.27 g/l × h; Qlev = 0.32, 0.29 and 0.12 g/l × h, respectively. However, the specific productivity of biomass for product synthesis was higher in fermentation systems with untreated stainless steel surfaces, probably due to some loss of physiological activity of cells attached to a modified carrier. Investigations of throughly washed activated stainless steel wire surfaces, by scanning electron microscopy after immobilization, showed significant attachment of cells to the carriers. A polymer layer covered the wire surface treated with TiCl4 after fermentations. This may be explained as the binding of extracellular polysaccharide, such as the fructose-polymer levan and yeast extract components, to the modified support via chelation. After four fermentations, craters and holes in the polymer layer were evident, probably as a result of CO2 formation. A small number of cells appeared on this layer. In view of the good ethanol formation during all fermentation cycles, it is probably that active Z. mobilis cells remained under the polymer layer. Wire treatment with AS resulted in the formation of long filamentous cells during fermentation and some disturbance of cellular fission. This may be partly explained by strong electrostatic interactions between the positively charged carrier surface and the predominately negatively charged surface of Z mobilis cells. However, this did not significantly affect other cellular functions. The surface of the wire treated with AG was practically without a polymer layer.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180310
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  • 5
    Electronic Resource
    Electronic Resource
    Influence of oxygen on the degradation of diesel fuel in soil bioreactors (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 109-122 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: In fixed-bed bioreactors, the influence of the oxygen content in the inlet air on the biodegradation of diesel fuel in unsaturated soil/compost mixtures was analyzed at 30°C over a period of 7 weeks. Firstly, a wide range from 0 to 80 vol.% O2 was investigated. Subsequently, the range below 5 vol.% O2 was examined more closely. Over the whole test period of seven weeks, no significant influence of oxygen could be observed above 1 vol. % O2 in the inlet air - either on the decrease of the total contaminants or on the total mineralization. Anaerobic conditions should be avoided for the degradation of diesel fuel. During the test period, the courses of CO2 production varied significantly depending on oxygen supply. Furthermore, a model was developed to estimate the total mineralization as a function of oxygen supply. More investigations are recommended in order to test this model for practical application.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180205
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  • 6
    Electronic Resource
    Electronic Resource
    Influence of some physicochemical factors on the viscosity of aqueous levan solutions of Zymomonas mobilis (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 167-174 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Zymomonas mobilis strain 113 “S” produces levan - an extracellular, viscous, biologically active, non-toxic fructose polymer with a unique structure and extraordinary properties. This polysaccharide was isolated at two different degrees of purity by alcohol precipitation from aqueous solutions and was characterized with respect to some rheological properties and stability of viscous solutions.The effects of temperature, pH and salt concentration on the viscosity of 1-3% levan solutions were examined. The viscosity of levan solutions was found to be quite stable and reversible at room temperature over a wide range of pH from 4 to 11. The viscosity was slightly affected by increased salt concentration. Levan solutions were rather stable at high temperatures (up to 70°C, 1 h, pH 6), where the viscosity could be almost completerly restored (up to 80-100%). Therefore, the degradation of the polymer structure under these conditions is probably insignificant. Temperatures of 70-100°C with a pH of less than 3.5 caused irreversible degradation of the levan structure.The above-mentioned properties of levan, obtained from Zymomonas mobilis 113 “S”, demonstrated the potential for the development of various therapeutic forms of pharmacologically-active levan and their application in medicine as well as in the food and other industries.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180214
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  • 7
    Electronic Resource
    Electronic Resource
    First announcement (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 176-176 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180216
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  • 8
    Electronic Resource
    Electronic Resource
    The extractive purification of peroxidase from plant raw materials in aqueous two-phase systems (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 179-188 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The extractive purification of peroxidase from Armoracia rusticana roots and Glycine max seed coats in temperature-induced and affinity microsphere-containing aqueous two-phase systems was stuied. The extractive purification of peroxidase from Glycine max seed coats was carried out in a temperature-induced aqueous two-phase system formed by Triton X-45, Triton X-100 and sodium acetate at pH 5.5 A 99% yield with a 6-fold purification factor was obtained. When the clear top phase was subjected to concanavalin-A affinity chromatography, the purification factor rose to 41 and the yield dropped to 28%.A two-step purification process for peroxidase from Armoracia rusticana roots was developed by adding concanavalin-A affinity microspheres to a PEG/phosphate aqueous two-phase system. The method allows a 60% recovery of high purity peroxidase (1,860 guaiacol units per mg). A lower recovery rate and degree of purification of this enzyme was achieved after temperature-induced aqueous two-phase partition or acetone precipitation and concanavalin-A affinity column chromatography.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180302
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of microbial endo-β-glucanase immobilized in alginate beads (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 189-200 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Endo-β-glucanase (endo-β-1,4-glucano-glucanase EC 3.2.1.4), isolated from Trichoderma reesei, was immobilized in calcium alginate beads, retaining 75% of its original activity. The polyanionic moiety surrounding the immobilized enzyme displaced the pH-activity profile to alkaline regions with respect to that of the free enzyme. The enzyme was inhibited by carboxymethylcellulose, but this inhibition appeared to be decreased by immobilizatíon. The enzyme immobilized in alginate beads showed a Km value (1.02% w/v) lower than that of the enzyme (1.31%). The apparent Vmax of immobilized cellulase preparations (238.3 μmol glucose/ml × h) decreased by a factor of 0.59 with respect to that of the soluble enzyme. The optimum temperature (60°C) of the free and entrapped enzymes remained unaltered. In contrast, the half-life of the endoglucanase immobilized in calciumalginate beads was 4.6 h at 55°C and 5.4 h at 60°C, while that of the free enzyme was 3.0 h at 55°C and 1.2 h at 60°C. A technological application of the immobilized enzymes was tested using wheat straw as a source of fermentable sugars. The hydrolytic degradation of straw, by means of a crude extract of free and immobilized cellulases and β-glucosidase, released a large amount of reducing sugars from wheat straw after 48 h (between 250-720 mg glucose/g straw), carrying out more than a 90% saccharification. A mixture of immobilized β-glucosidase and free cellulases maintained 80% of the activity of the soluble counterparts, and the co-immobilization of both types of enzymes reduced by hydrolytic efficiency to half.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180303
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  • 10
    Electronic Resource
    Electronic Resource
    Performance of airlift bioreactors in the cultivation of some antibiotic producing microorganisms (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 201-229 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The specific aspects of airlift reactors emphasizing their function relevance to particular application as bioreactors are presented.The two main groups of airlift reactors - external-loop and concentric-tube reactors - were investigated on a pilot-plant scale with regard to their performance during the cultivation of unicellular and filamentous microorganisms which produce Bacitracin, Cephalosporin C and Nystatin. Some results were compared to those obtained in conventional stirred tank bioreactors. The comparison was carried out based on physical properties (oxygen transfer rate (OTR), volumetric mass transfer coefficient (kLa) and efficiency of oxygen transfer (EO2)), cell mass, productivity and substrate consumption, secondary metabolite production, and efficiency of the product formation with regard to the specific power input.It was shown that B. licheniformis, C. acremonium and S. noursei fermentations occurred similarly to those performed in stirred vessels, proving that the capacity of the airlift bioreactors surpassed the problems which arise from the morphology and rheology of the broths. From the chemical engineering point of view, it was obvious that the primary tasks of a bioreactor (uniform distribution of microorganisms and nutrients over the entire fermenter volume, appropriate supply of biomass with nutrients and oxygen) were fulfilled by the airlift bioreactors tested. In addition, the efficiency of oxygen transfer (OTR referred to power input) in the airlift fermenters proved to be about 38% higher than in the stirred tank bioreactors (expressed as average values), while the sorption efficiency (OTR referred to antibiotic production) was found to be 22% greater in the airlift system than in an STR.Therefore, the biosyntheses were performed with about a 30-40% increase in energy efficiency and energy savings compared to the conventional system.Moreover, the lack of mechanical devices in the airlift system provides greater safety and a gentler environment for the cultivation of microorganisms.
    Additional Material: 18 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180304
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  • 11
    Electronic Resource
    Electronic Resource
    Detection of chlorocatechol 1,2-dioxygenase genes in proteobacteria by PCR and gene probes (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 231-240 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: In various bacterial strains belonging to the β-subdivision of proteobacteria which are capable of degrading chlorinated monoaromatic compounds, chlorocatechol 1,2-dioxygenase genes were detected by PCR and Southern hybridization. Using PCR primers derived from the conserved sequence motifs of chlorocatechol 1,2-dioxygenase genes tfdC, clcA and tcbC, PCR products of the expected size were obtained with the test strains, but not with negative control strains. The specificity of the PCR products was verified by hybridization using an oligonucleotide probe for an internal sequence motif which is evolutionarily conserved among chlorocatechol 1,2-dioxygenases and some other dioxygenases that catalyze the intradiol aromatic-ring-cleavage. Hybridization with the tfdC PCR product from the 2,4-D degradative plasmid pJP4 under stringent conditions revealed different extents of homology of the chlorocatechol 1,2-dioxygenase genes to the canonical tfdC sequence in the various strains. These findings were confirmed by the nucleotide sequence analysis of the tfdC-specific PCR products. From our results, we conclude that the PCR primer set is more suitable than the hybridization with pJP4-derived gene probes for the detection of diverse chlorocatechol 1,2-dioxygenase genes in proteobacteria.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180306
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  • 12
    Electronic Resource
    Electronic Resource
    Production of extracellular enzymes by two Pleurotus species using banana pseudostem biomass (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 243-254 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The degradation of lignocellulosic biomass of banana pseudoste was investigated during solid state fermentation (SSF) by P. ostreatus and P. sajor-caju. Both organisms proved to be efficient degraders of banana pseudostem biomass. P.ostreatus degraded hemicellulose (40% of dry weight, d.w.) better than cellulose (17.5% of d.w.) and lignin (10% of d.w.). P. sajor-caju also degraded hemicellulose (31% of d.w.) better than cellulose (12.4% of d.w.) and lignin (6% of d.w.). In both cases, a preferential removal of hemicellulose during the initial growth period and a delayed degradation of lignin were observed. The kinetics of cellulolytic, hemicellulolytic and lignolytic enzyme production in liquid culture were also examined. The activities of CMCase and β-glucosidase were highest at 16 days of growth and avicelase activity was at its maximum after 24 days (CMCase - 1.1 IU/ml, β-glucosidase - 0.09 IU/ml in the case of P. ostreatus; CMCase - 1.0 IU/ml, β-glucosidase - 0.087 - IU/ml in the case of P. sajor-caju.). Xylanase and laccase activity reached their maximum after day 16 and day 24 of incubation, respectively. (Xylanase - 1.1 IU/ml and laccase 3.0 IU/ml in the case of P. ostreatus; xylanase - 1.0 IU/ml and laccase - 3.6 IU/ml in the case of P. sajor-caju.). The efficient degrading capacity of test fungi demonstrated their potential use in the conversion of banana pseudostem biomass into mycelial protein-rich fermented animal feed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180309
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  • 13
    Electronic Resource
    Electronic Resource
    Conference announcement (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 275-276 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180313
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  • 14
    Electronic Resource
    Electronic Resource
    Preparation and some properties of multinucleate cells of Saccharomyces cervisiae after colchicine treatment (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 305-313 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: For the purpose of forming cells possessing more than three nuclei and of determining the factors inducing multinucleation, cells of Saccharomyces cerevisiae were treated with 0, 0.3, 0.5, and 1.0% [w/v] colchicine solution, with and without shaking. When the cells were treated with 1.0% [w/v] colchicine solution, the number of cells containing two to eight nuclei was the largest. The multinucleate cells could grow on potato dextrose agar medium and their multinucleate nature did not disappear for at least three generations. This means that such cells are genetically stable. The proliferation rate of the multinucleate cells was not superior to that of the original strain. However, by monitoring the weight loss of the flask, it was possible to indirectly estimate the increase in the alcohol production of the multinucleate cell. It was concluded that the shaking treatment and higher colchicine concentrations contributed to multinucleation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180403
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  • 15
    Electronic Resource
    Electronic Resource
    Mixed-solid substrate fermentation. A novel process for enhanced lipase production by Candida rugosa (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 315-324 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Candida rugosa was cultivated in a mixed-solid substrate containing coconut oil cake (COC) and fine and coarse wheat bran (1:1:1) with an initial water activity (aw) of 0.92. The substrate was modified by adding a mineral solution (5%), corn steep liquor (6%), maltose (2%), peptone (3%), olive oil (10%), gum arabic (0.4%), different fatty acids (0.3%) and Tweens (0.5%). Fermentation in a column fermenter significantly improved the lipase yield to 118.2 Units per gram of dry fermented substrate [U/gds] at 72 h. This result was obtained 24 hours earlier than in our former studies (87.76 U/gds at 96 h) in COC, and the yield showed a 38% increase. Growth was measured indirectly by determining the glucosamine content in the cell wall of the yeast contained in the fermented matter, after its hydrolysis.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180405
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  • 16
    Electronic Resource
    Electronic Resource
    Production of indole acetic acid in root nodules and culture by a Rhizobium species from root nodules of the fodder legume Melilotus alba DESR. (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 53-62 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The root nodules of Melilotus alba DESR., a fodder legume, contained high amounts of IAA. A tryptophan pool present in the nodule might serve as a source of IAA production. Presence of IAA oxidase and peroxidase in the nodules indicated the metabolism of IAA, at least in part, in the nodules. The Rhizobium species isolated from the root nodules produced a high amount of IAA (190 μg/ml) from L-tryptophan supplemented basal medium. IAA production and microbial growth were coincident. The production of IAA by the Rhizobium sp. was increased by 315% when the medium was supplemented with lactose (1%), NiCl2 (10 μg/ml), cetyl pyridinium chloride (0.5 μg/ml) and glutamic acid (0.4%), in addition to L-tryptophan (3 mg/ml). The possible role of the rhizobial production of IAA on the rhizobia-legume symbiosis is discussed.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180110
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  • 17
    Electronic Resource
    Electronic Resource
    A comparison of methods for DNA extraction from paraffin-embedded tissue for microsatellite instability analysis by polymerase chain reaction (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 77-83 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: In a prospective study, nuclear DNA was extracted from colorectal tumours and normal mucosa which had been fixed in buffered formalin and embedded into paraffin. DNA-extraction was performed using three different methods: a commercial kit which was not especially created for this use; a known fast procedure without DNA-cleaning steps; and a more conventional DNA-preparation protocol with DNA-cleaning. Using the polymerase chain reaction (PCR), DNA was amplified by being targeted onto two β-globin fragments with different lengths (536 bp and 989 bp) and (CA)n repeats localized on chromosome 5q (D5S346) and chromosome 17p (TP53CA) with a length of about 100 bp for detection of microsatellite instability. The success rate of microsatellite amplification was 100% with all methods. The 536 bp β-globin fragment could be amplified with a success rate ranging from 40% to 100%. The amplification of the 989 bp β-globin fragment was unsuccessful. Significant differences were observed between the three methods in the final DNA concentration and DNA yield. In microsatellite instability studies of paraffin-embedded tissues, the investigator can expect a high success rate of nearly 100% using any of the described methods.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180113
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  • 18
    Electronic Resource
    Electronic Resource
    Erratum (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 92-92 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180116
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  • 19
    Electronic Resource
    Electronic Resource
    Umweltbiotechnologie. Berlin, Heidelberg, New York, Paris, Tokyo, Hong Kong: Springer Verlag, 217 pages, 69 figures, 16 tables; DM 88.00. ISBN 3-540-61423-0 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 108-108 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180204
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  • 20
    Electronic Resource
    Electronic Resource
    Enzymatic decrease in the phenolic content of canola meal using concentrated aqueous or aqueous/hexane slurries (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 95-106 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: An enzymatic process to decrease the phenolic content in canola meal was investigated. The new method was based on the addition of an enzyme preparation from the white-rot fungus Trametes versicolor to concentrated meal-buffer slurries. This approach eliminated the extraction of the valuable meal components such as proteins and carbohydrates. Two systems were considered: (i) slurries with canola meal concentrations higher than 33% [w/v]; (ii) slurries with canola meal concentrations equal to or less than 12.5% [w/v] with n-hexane as the main component of the continuous phase.The concentration of sinapic acid esters decreased by 99% after a 1.5, 2 and 3 hour long treatment of the meal with an initial moisture content of 75% at 90°C, 70°C and 50°C, respectively. The process was carried out at temperaturs as high as 110°C. Both the enzyme and the moisture concentrations influenced the enzymatic process and their action was coupled. The concentration of oxygen strongly affected the process.The enzymatic process was able to be carried out in the presence of hexane as the main component of the continuous phase. The optimum temperature for such a process was 30-40°C, At 30°C, after 1 h of treatment, the meal phenolic content was decreased by 97%. The water uptake by the meal was diminished in the presence of hexane.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180202
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  • 21
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    Electronic Resource
    Growth of Paenibacillus larvae, the causative agent of American foulbrood in honey bees and Bacillus popilliae, the causative agent of milky disease in beetle larvae in lepidopteran cell cultures (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 123-133 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: TNM-FH Lepidopteran insect cell culture medium containing 10% fetal bovine serum (FBS), while allowing limited vegetative growth of Paenibacillus larvae (wild-type strain), the causative agent of American foulbrood, contained no viable vegetative cells upon subculture, nor were any heat resistant spores produced in this medium alone. However, TNM-FH medium cotaining embryonic or midgut cells from Trichoplusia ni, hemocytes from Estigmene acrea, ovarian and embryonic cells from Spodoptera frugiperda, embryonic cells from Plutella xylostella, Spodoptera exigua and Pseudaletia unipuncta or ovarian cells from Lymantria dispar, supported both heavy vegetative cell growth and moderate production of heat resistant spores. EX-CELL 405 serum-free insect cell culture medium alone appeared to contain the appropriate nutrients required for both vegetative growth and sporulation of P. larvae. However, in the presence of embryonic cells from T. ni, limited vegetative growth occurred and the P. larvae cells appeared to die off. This was confirmed by the fact that no colony growth occurred upon subculture, nor were any heat resistant spores detected. This was true also in the presence of fat body cells from T. ni, except that a limited number of spores (4,000/ml) were detected in the form of cology-forming units (CFU) on plates following heating to 80°C for 20 minutes. In a parallel study with a wild-type strain of Bacillus popilliae, vegetative cells grew only in TNM-FH medium in the presence of mid-gut BTI-Tn-MG and ovarian (Tn-368) cells of T. ni. No heat resistant spores, however, were detected in any of the cultures. When BTI-Tn-MG and Tn-368 cells were further challenged with four variant cultures of B. popilliae, vegetative growth and limited sporulation were achieved. The BTI-Tn-MG cell line in TNM-FH medium produced as many as 12,000 spores/ml after 21 days in culture.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180206
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  • 22
    Electronic Resource
    Electronic Resource
    Ethanol production from native cassava starch by a mixed culture of Endomycopsis fibuligera and Zymomonas mobilis (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 149-155 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The conversion of starch from unhydrolyzed cassava flour to ethanol by a pure culture of Endomycopsis fibuligera and by a co-culture of this amylolytic yeast and the bacterium Zymomonas mobilis was studied.The best overall results were obtained using the mixed culture. After 96 h of fermentation of a medium containing 150 g/l initial cassava starch, an ethanol concentration of 31.4 g/l, a productivity of 0.33 g ethanol/l × h and a yield of 0.21 g ethanol/g initial starch were reached. The highest yield (0.37 g/g) was obtained after 48 h when using a medium containing 50 g/l initial starch.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180211
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  • 23
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    Electronic Resource
    Cosmetic microbiology. A practical handbook. Boca Raton, New York: CRC Press LLC, 1997, 323 pages, 6 figures, 18 tables, hardcover DM 185.00. ISBN 0-8493-3713-5 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 175-176 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180215
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  • 24
    Electronic Resource
    Electronic Resource
    Masthead (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998) 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180301
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  • 25
    Electronic Resource
    Electronic Resource
    Handbuch des Umweltschutzes und der Umweltschutztechnik. Additiver Umweltschutz: Behandlungj von Abwässern (Volume 4). Berlin, Heidelberg, New York, Barcelona, Budapest, Hong Kong, London, Milan, Paris, Santa Clara, Singapore, Tokyo: Springer Verlag. XXVIII + 701 pages, 381 pages, 381 figures, 107 tables; DM 118.00. ISBN 3-540-58061-3 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 230-230 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180305
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  • 26
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    Electronic Resource
    Bioreaction engineering. Volume 3: Bioprocess monitoring. Chichester, New York, Weinheim, Brisbane, Singapore, Toronto: John Wiley & Sons, 1997, 389 pages, 204 figures, 84 tables; hardcover DM 98.00. ISBN 0-471-97061-1 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 28-28 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180104
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  • 27
    Electronic Resource
    Electronic Resource
    Growth patterns of yeast colonies depending on nutrient supply (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 17-27 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Common theories of microbial growth and physiology are formulated exclusively in terms of the isolated microorganisms - especially bacteria. This is, however, an inadmissible simplification because it is obvious that the organization of microbial populations and colonies follows certain general rules.Bacterial colonies are able to generate complex interfacial growth patterns similar to those observed during diffusion-limited growth processes in non-living systems. One reason for these patterns is assumed to be the ability of many bacteria to swarm in an active manner on a substrate surface. Therefore the models of bacterial colony growth incorporate “random walkers”, which move actively in response to a gradient in the concentration of nutrients and communicate with each other by means of a chemotactic feedback.A selected number of yeasts were tested with regard to their colony growth patterns depending on the medium parameters such as nutrient concentration. Growth patterns similar to those which were described in literature for bacteria were also found in these experiments. It concerns in particular growth types like compact growth, fractal growth and dense-branching growth.This result allows a hypothesis to be formulated, that - especially in the case of fractal growth patterns - wandering of cells on a substrate surface may be induced by uncontrolled “swimming” on a thin water film caused by the metabolic activity (e.g. respiration) of the cells on the surface of the agar.Furthermore it was found that an interplay between changes in the individual morphology of yeast cells and the morphology transitions takes place. Such growth patterns are known for Candida sp. which are able to form pseudomycel and blastospores.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180103
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  • 28
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    Electronic Resource
    Selective detectors. Environmental, industrial, and biomedical applications. New York, Chichester, Brisbane, Toronto, Singapore: John Wiley & Sons, Inc., 1997, XXI + 261 pages, 94 figures, 18 tables, 5 schemes; £ 49.95. ISBN 0-471-01343-9 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 42-42 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180106
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  • 29
    Electronic Resource
    Electronic Resource
    Development of toxicity tolerant water hyacinth (Eichhornea crassipes) for effective treatment of raw sewage (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 43-50 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pioneering research efforts in the handling of municipal sewage in developing countries have involved the use of water hyacinth (Eichhornea crassipes) to purify sewage for possible re-use of the effluent water for domestic purposes. The ability of water hyacinth to remove pollution from raw sewage has been found to be impaired by sewage toxicity. Trials were therefore carried out to adapt water hyacinth to toxicity and thereby increase its ability to remove pollutants from raw sewage. The plants were adapted using an active bio-degrader consisting of Pseudomonas aeruginosa, Escherichia coli, Klebsiella ozaenae, Klebsiella edwardsiella and Baccillus subtilis. The adaptation progressed through 20, 40, 60 and 80% sewage dilution until plants capable of growth in 100% raw sewage were obtained. Plants were observed for morphological growth and at four weeks, samples were collected for tissue analysis.The plants progressively absorbed nutrients from sewage up to the fourth week, when signs of toxicity were obsereved through wilting, loss of turgidity and reduction in leaf number. However, plants that survived through a series of adaptations under various sewage dilutions exhibited luxuriant growth on raw sewage. In synergy with the active bio-degrader, the efficiency of the adapted water hyacinth to remove pollutants (nutrients) from raw sewage was enhanced by 93%.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180107
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  • 30
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    Electronic Resource
    Nonconventional yeasts in biotechnology. A handbook. Heidelberg, New York, London, Paris, Tokyo, Hong Kong: Springer-Verlag Berlin, 1996, 619 pages, 94 figures, 45 tables; DM 128.00. ISBN 3-540-59482-5 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 84-84 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180114
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  • 31
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    Electronic Resource
    Microbially influenced corrosion of materials. Scientific and engineering aspects. Berlin, Heidelberg, New York, London, Paris, Tokyo, Hong Kong: Springer Verlag, 475 pages, 208 figures, 56 tables; hardcover DM 168.00. ISBN 3-540-60432-4 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 134-134 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180207
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  • 32
    Electronic Resource
    Electronic Resource
    Masthead (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998) 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180101
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  • 33
    Electronic Resource
    Electronic Resource
    Cell reuse in submerged lactic acid batch fermentation (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 3-16 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The reusability of biomass in lactic acid batch fermentation with free cells of Lactobacillus paracasei was studied in a 2-1 fermenter and in a 50-1 fermenter. In lab-scale fermentation experiments, 33 to 100% of the cell mass formed was reused in the subsequent batch in each case. In a series of seven consecutive batches, maximum values of lactate formation productivity of 6.32 to 11.54 g/l × h were observed at initial cell concentrations of 2.1 to 24.6 g/l. In all of the experiments, the initial cell viability was 78% or greater than 78%, and the final cell viability did not fall below 70%. At cell concentrations above 20 g/l, the productivity of lactic acid formation did not increase further, but remained constant. Because its level could be influenced by varying the proportions between the content of yeast extract, peptone and initial cell mass (1:1:2, 1:1:1 and 3.3.1) in the medium and no inhibitory effects were observed, this finding can be attributed to nutrient limitation. A low degree of cell reuse was reached in an analogous series of experiments carried out in a 50-1 fermenter. In this case, the initial cell concentration varied between 0.5 and 1.1 g/l, and therefore cell growth was not limited by nutrients in the first period of fermentation. Lactate production was still stable after six cell-reuse operations. The lactic acid yield did not fall below 90%. Temporary storage of the biomass in a refrigerator for a time interval of one to two weeks caused no significant impairment of overall lactate production, but a proportional prolongation of the lag phase occurred with increasing duration of storage.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180102
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  • 34
    Electronic Resource
    Electronic Resource
    Growth kinetics of the 4-nitrophenol degrading strain Pseudomonas putida PNP1 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 29-41 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A 4-nitrophenol degrading strain PNP1 isolated from the El-Harrach River near Algiers (Algeria) was studied with respect to its growth behaviour. According to the morphological and biochemical characteristics this strain was assigned to Pseudomonas putida. Besides 4-nitrophenol, the strain also used 1,2- and 1,4-dihydroxybenzene, benzoate, 4-hydroxybenzoate and 3,4-dihydroxybenzoate as sources of carbon and energy, degrading them exclusively via the ortho pathway. Pseudomonas putida PNP1 degrades 4-nitrophenol through a purely oxidative pathway with release of the nitro group as nitrite. During cultivation with 4-nitrophenol in ammonium-containing mineral medium, the strain PNP1 grew optimally at pH 7 and at a temperature between 30 and 35°C and showed stoichiometric nitrite release (at pH 7 and 30°C MONOD model parameters μmax = 0.615 h-1 and KS = 0.145 mg/l). A phenomenological model for the description of growth inhibition at high 4-nitrophenol concentrations was derived (below 400 mg/l only weak inhibition and at 600 mg/l acute toxicity). In ammonium-free medium, the maximum specific growth rate was reduced to 0.318 h-1 and part of the 4-nitrophenol-N was used as the nitrogen source (32% N in biomass and 68% N in nitrite). The yield coefficients of strain PNP1 were smaller in ammonium-free than in ammonium-containing medium (e.g. with 4-nitrophenol YX/S = 0.305 g/g compared to 0.350 g/g), which can be explained by the energy expense for the assimilatory nitrite reduction in the biosynthesis of N-containing cellular compounds. But the oxygen consumption was only slightly influenced by the ammonium content of the cultivation medium (e.g. with 4-nitrophenol YO/S = 1.005 g/g compared to 0.954 g/g).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180105
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  • 35
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    Electronic Resource
    DNA sequencing strategies: Automated and advanced approaches. New York, Chichester, Brisbane, Toronto, Singapore, Weinheim: John Wiley & Sons, Inc. and Heidelberg, Berlin, Oxford: Spektrum Akademischer Verlag, 1997, 216 pages, 76 figures, 4 tables; £ 32.50 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 51-51 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180108
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  • 36
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    Electronic Resource
    Bacteria in biology, biotechnology and medicine. (Third edition). Chichester, New York, Brisbane, Toronto, Singapore: John Wiley & Sons Inc. IX + 319 pages, 90 figures, 13 tables, 10 plates. ISBN 0-471-95811-5 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 52-52 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180109
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  • 37
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    Biokatalysatoren und Enzymtechnologie. Weinheim, New York, Basel, Cambridge, Tokyo: VCH Verlagsgesellschaft mbH, 1997, 344 pages, 150 figures, 62 tables; DM 78.00. ISBN 3-527-28238-6 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 76-76 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180112
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  • 38
    Electronic Resource
    Electronic Resource
    Purification and immobilization of dextranase (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 63-75 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: An enzymic characteristic of Novo dextranase was presented. In addition to a high dextranolytic activity (7,200 U/ml), the crude enzyme also contained small amounts of protease, glucoamylase, polygalacturonase, carboxymethylcellulase, laminarinase and chitinase. A highly purified dextranase was then simply separated from a commercial preparation by column chromatographies on DEAE-Sepharose, CM-Sepharose, and by chromatofocussing on Polybuffer Exchanger PBE-94. The enzyme was recovered with an over 200-fold increase in specific activity and a yield of 84%. The final preparation was homogeneous, as observed during high performance liquid chromatography (HPLC). Size-exclusion HPLC indicated that dextranase had a molecular mass of 35 kDa and its isoelectric point, established by chromatofocussing, was 4.85. Analysis of the dextran break-down products indicated that purified dextranase represents an endolytic mode of action, and isomaltose and isomaltotriose were identified as the main reducing sugars of dextran hydrolysis. The enzyme was then covalently coupled to the silanized porous glass beads modified by glutaraldehyde (Carrier I) or carbodiimide (Carrier II). It was shown that immobilization of dextranase gave optimum pH and temperature ranges from 5.4 to 5.7 and from 50°C to 60°C, respectively. The affinity of the enzyme to the substrate decreased by a factor of more than 13 for dextranase immobilized on Carrier I and increased slightly (about 1.4-times) for the enzyme bound to Carrier II.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180111
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  • 39
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    Electronic Resource
    Biodegradability of lignosulphonate by Streptomyces viridosporus strain T7A and a mixed natural microbial population antagonistic effects (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 85-91 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The ability of a mixed natural microbial population, collected in an aerated lagoon treating Fluff pulp effluent and Streptomyces viridosporus strain T7A, to degrade lignosulphonate was evaluated. S. viridosporus growing in a mineral medium containing glycerol (7 g/l) and lignosulphonate (1 g/l) allowed 20% of lignosulphonate to be degraded after 18 days of incubation. A culture of the mixed population on culture medium after S. viridosporus growth was unable to degrade lignosulphonate products. Moreover, antagonism between S. viridosporus and the mixed population or between S. viridosporus and the isolated strains from this population was observed. The enhancement of lignosulphonate biodegradation by naturally occurring microorganisms in association with S. viridosporus (bioaugmentation strategy) seems to be difficult.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180115
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  • 40
    Electronic Resource
    Electronic Resource
    Masthead (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998) 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180201
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  • 41
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    Electronic Resource
    Handbuch des Umweltschutzes und der Umweltschutztechnik. Vol. 1: Emissionen und ihre Wirkungen. Berlin, Heidelberg, New York, Barcelona, Budapest, Hong Kong, London, Milan, Paris, Santa Clara, Singapore, Tokyo: Springer-Verlag GmbH XXX + 842 pages, 169 figures, 121 tables; DM 118.00 ISBN 3-540-58584-2 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 106-107 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180203
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  • 42
    Electronic Resource
    Electronic Resource
    Masthead (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998) 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180401
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  • 43
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    Electronic Resource
    Yeast physiology and biotechnology. Chichester, New York, Weinheim, Brisbane, Singapore, Toronto: John Wiley & Sons, Ltd. 350 pages; £ 29.95. ISBN 0-471-96447-6 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 314-314 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180404
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  • 44
    Electronic Resource
    Electronic Resource
    Microbial cleaning of waste gas containing volatile organic compounds in a bioreactor system with a closed gas circuit (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 291-304 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The cleaning of the exhaust gases of a bioreactor containing volatile hydrocarbons in a bioreactor system with a closed gas circuit is described. The bioreactor system consisted of three different reactor types: a stirred tank which was filled with hydrocarbon-containing waste water to simulate the exhaust gases of a remediation process; a trickle-bed reactor for aerobic treatment of the exhaust gas from the stirred tank; and a photoreactor containing an algae culture which assimilated CO2 from the trickle-bed reactor and also produced O2. With this bioreactor system, it was possible to efficiently remove volatile organic compounds (VOC) from the waste gases. Depending on the type of waste water investigated, elimination rates of 41% to 93% of BTEX (benzene, ethylbenzene, toluene, xylene) and 29% to 53% of VCH (volatile chlorinated hydrocarbons) were obtained. Due to the photosynthesis of the algae in the system's photoreactor, oxygen concentrations between 12% and 18% [v/v], equivalent to about 57% to 83% DOT, were obtained. This concentration permitted the aerobic degradation to be carried out without having to add fresh air. The trickle-bed reactor and the photoreactor worked continuously, whereas the waste water in the stirred bioreactor was replaced in different batches. The accumulation of toxic compounds in the nutrient solutions of the trickle-bed (EC-50 〉 30 g/l) and of the photoreactor (EC-50 〉 35 g/l) was low. Carbon dioxide concentrations in the gas flow were higher than in fresh air (1% to 3% [vol/vol]), but no long-term accumulation of CO2 occurred. This means that the algae in the photoreactor were active enough to assimilate the CO2 which had been produced. They were also able to produce sufficient oxygen for aerobic hydrocarbon degradation. The system described is a first step towards treating waste gases which results from the bioremediation of hydrocarbon-contaminated media in a closed gas circuit without any emission (e.g. VOC, CO2, germs).
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180402
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  • 45
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    Forschungsethik. Gentechnik und neue Biotechnologie. Stuttgart: Wissenschaftliche Verlagsgesellschaftj mbH, 411 pages; DM 96.00. ISBN 3-8047-1452-8 (WVG) (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 325-326 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180406
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  • 46
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    Electronic Resource
    Yeasts in natural and artificial habitats. Berlin, Heidelberg, New York, Barcelone, Budapest, Hong Kong, London, Milan, Paris, Santa Clara, Singapore, Tokyo: Springer Verlag. IX + 381 pages, 59 figures, 28 tables; DM 198.00. ISBN 3-540-56820-4 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 352-352 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180409
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  • 47
    Electronic Resource
    Electronic Resource
    Fusion of yeast protoplasts and isolated nuclei of Fusarium moniliforme (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 353-359 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Protoplasts of a xylose-fermenting yeast strain (a fusion product of Pachysolen tannophilus and Saccharomyces cerevisiae) were fused with isolated nuclei of the xylan degrading filamentous fungus Fusarium moniliforme. Polyethyleneglycol 4000 was used as the fusogenic agent. Fourteen stable hybrids showing xylanase activity were obtained. It can be assumed that this ability was acquired from the nuclear genome of the fungus, since the parental yeast strain did not show any xylanase activity. The enzymatic activity was determined quantitatively. The parental strain of the fungus reached its maximum xylanase activity of 796 nkat/ml at 96 h of growth. Four of the hybrids had a xylanase activity of between 211 and 297 nkat/l at 24 h of growth. Zymograms of these hybrids showed the presence of xylanases when grown on xylan as the sole carbon source. Using pulse field electrophoresis gels, no difference between the chromosome pattern of the fusion products and the parental yeast strain was observed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180410
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  • 48
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    Electronic Resource
    Dynamics of cell and tissue motion. Basel, Boston, Berlin: Birkhäuser, 1997, 352 pages; DM 118.00. ISBN 3-7643-5781-9 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 367-367 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180413
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  • 49
    Electronic Resource
    Electronic Resource
    Selection of hydroxyproline-resistant cell lines from Solanum Tuberosum L. Callus. II. Plant regeneration and frost tolerance of regenerated plants (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 361-366 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The calluses of two hydroxyproline-resistant lines (D20-1 and D30-1) of Solanum tuberosum L. were transferred to a solidified MS medium containing 1.0 mg/I IAA, 2.0 mg/l zeatin, 40.0 mg/l adenine sulphate, 1 g/l casein hydrolysate, 20 g/l sucrose and 10 g/l agar for plant regeneration. The shoot regeneration was only achieved from the callus of line D20-1. Regenerated shoots exhibited morphological variability. The degrees of frost tolerance were higher in the leaves of the regenerated plants compared with the leaves of the non-selected control plants, but lower than that of the callus from which they were regenerated.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180412
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  • 50
    Electronic Resource
    Electronic Resource
    Optimization of the growth parameters of Aspergillus foetidus (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 327-338 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The batch production of gluconic acid in the presence of glucose, sucrose and molasses was investigated using free mycelia of Aspergillus foetidus NRRL 337 in shake flasks. Eight growth parameters were chosen as independent variables. The temperature, pH, substrate type and initial concentrations, inoculum percentage and shake rate directly affected the specific microorganism growth and gluconic acid production rates. The optimum temperature and initial pH values were found to be 33°C and five to six, respectively. The maximum specific growth and gluconic acid production rates were established as 57 g/dm3 of glucose, 75 g/dm3 of sucrose and 150 g/dm3 of molasses. The optimum values of the shake rate, inoculum percentage and initial ammonium nitrate concentration were determined as 100 1/min, 0.5% and 1.5 g/dm3, respectively. The maximum gluconic acid concentrations corresponding to these initial substrate concentrations were observed to be 8.3 g/dm3, 17.4 g/dm3 37.0 g/dm3, respectively. The optimum specific microbial growth and gluconic acid production rates were found as 0.0145 1/h and 0.0375 g/g × h, respectively, for the fermentation conditions of SGo = 57 g/dm3, T = 28°C, initial pH = 6.5, N = 84 1/min, A = 0.5 g/dm3 and I = 0.5%.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180407
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  • 51
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    Electronic Resource
    Characteristics of immobilized thermostable amylases from two Bacillus licheniformis strains (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 339-351 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Covalent immobilization of thermostable α-amylases from catabolite resistant and sensitive Bacillus licheniformis strains on controlled pore glass (CPG) and porous silica (Spherosil) beads and ionic binding on DEAE-cellulose, Amberlite and Dowex were investigated. Preparations with satisfactory operational stabilities and activities up to 1,600 U/g of support (ionic binding) and 800 U/g carrier (covalent coupling) were obtained. Immobilization led to a narrowing of the pH interval of maximum activity. The fixed amylases were stable in limited pH regions around the optimum pH level. An enhancement of the enzyme thermostability was observed. Apparent shifts of the optimum temperatures were not found. The apparent Vmax decreased up to 80 times. The Km′ remained unchanged (for amylopectin as the substrate) or increased up to 10 times (soluble starch). Maltose, maltotriose and maltopentaose were the main products of the hydrolysis. A significant increase in maltopentaose content was observed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180408
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  • 52
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    Electronic Resource
    Handbuch des Umweltschutzes und der Umweltschutztechnik. Sanierender Umweltschutz (Volume 5). Berlin, Heidelberg, New York, Barcelona, Budapest, Hong Kong, London, Milan, Paris, Santa Clara, Singapore, Tokyo: Springer Verlag XXII + 410 pages, 117 figures, 30 tables; DM 118.00 ISBN 3-540-58062-X (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 359-360 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180411
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  • 53
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    Molecular biotechnology: Therapaeutic applications and strategies. Chichester, New York, Brisbane, Toronto, Singapore, Weinheim: Wiley-Liss (A John Wiley & Sons Inc. Publications), 223 pages, 37 figures, 5 tables; £ 34.95. ISBN 0-471-11681-5 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 147-147 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180209
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  • 54
    Electronic Resource
    Electronic Resource
    Immobilization of glucoamylase on polyamide nets (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 135-146 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The formation of reactive groups on polyamide nets (nylon 6) and the subsequent immobilization of glucoamylase were investigated. Different mesh sizes of the nets and two chemical methods of enzyme coupling - i( partial hydrolysis of the polyamide with subsequent glutaraldehyde binding and ii) O-alkylation of the carrier using a treatment with a benzene-methyl sulphate mixture - were used. The reactivity of immobilized glucoamylase (GA) was tested by hydrolysis reactions using 1% starch solutions. The highest reactivity (140 μg glc/)min × cm2 was obtained for methylated nylon samples attached to a glass rod and by coupling glucoamylase on the nylon surface which had been treated with lysine and glutaraldehyde. This method resulted in a more reactive and more stable preparation of immobilized glucoamylase as compared to a simpler method of coupling glutaraldehyde to partially hydrolyzed nylon.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180208
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  • 55
    Electronic Resource
    Electronic Resource
    Book announcement (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 148-148 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180210
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  • 56
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    Electronic Resource
    Biochemische Labormethoden (2nd revised edition). Berlin, Heidelberg, New York, London, Paris, Tokyo, Hong Kong, Barcelona, Budapest: Springer-Verlag GmbH, XIV + 249 pages, 15 figures, 72 tables; DM 48.00. ISBN 3-540-58584-2 (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 156-156 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180212
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  • 57
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    Electronic Resource
    Culture conditions for the production of pectinolytic enzymes by the white-rot fungus Trametes trogii on a laboratory scale (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 157-166 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Different cultural parameters that regulate pectinolytic enzyme production in vitro by Trametes trogii were studied. When grown in a medium containing pectin, T. trogii produced extracellular polymethylgalacturonase, polygalacturonase and pectin lyase but no pectate lyase activity. No significant differences in the maximum enzyme activities measured were observed with the addition of xylan, carboxymethylcellulose or both to the medium containing pectin. The addition of glucose to that medium considerably decreases all the activities studied, and in a medium with glucose as the sole carbon source no galacturonase activity could be measured, and pectin lyase activity was at its minimum. The low synthesis of pectin lyase in cultures containing glucose suggests that this enzyme is constitutive in contrast to the polygalacturonases that were not detected. The increase in pectin concentration stimulated growth and enzyme production. The highest specific activities were attained with the greatest concentration tested (15 g/l). Casamino acids were the best nitrogen source for enzyme production. Maximum growth was measured at pH 3.3; pH values of around 4.5 stimulated enzyme production, but high pectinase activities were also detected in media with more alkaline initial pH values (6.2 for galacturonases and 6.6 for lyases), probably owing to the specific induction of particular isoforms. In the range of 23 to 28°C, good results were obtained in growth as well as in enzyme production. The addition of Tween 80 promoted growth and gave the highest yield of polymethylgalacturonase and pectin lyase (0.37 and 36.2 E.U./ml, respectively). The highest polygalacturonase activity (1.1 E.U/ml) was achieved with polyethylene glycol. Tween 20 and Triton X-100 inhibited growth and pectinase production.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180213
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  • 58
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    Electronic Resource
    Influence of different vitamin-nitrogen sources on cell growth and propionic acid production from sucrose by Propionibacterium shermanii (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 267-274 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cell growth and organic acid production by Propionibacteria are dependent on the vitamin-nitrogen source in the culture medium. Final cell and propionic acid concentrations produced by Propionibacterium shermanii, using corn-steep liquor, were higher than those obtained utilizing yeast extracts. Since corn-steep liquor is much cheaper than yeast extract, the process becomes more attractive. By calculating the specific growth rates, it was observed that the critical propionic acid concentration, that prevents all growth (μX = 0), is different depending on the vitamin-nitrogen source used and its concentration. For example, for 5.0 and 15.0 g/l Oxoid yeast extract, those critical propionic acid concentrations were 16.0 and 27.0 g/l, respectively. Such propionic acid concentrations inhibit the cell growth, but not the formation of acid. The specific propionic acid production rate also indicates that the critical concentration for metabolic activity, when propionic acid is no longer produced (μP = 0), varies according to the vitamin-nitrogen source and its concentration in the medium. For 5.0 and 15.0 g/l Oxoid yeast extract, those concentrations were 22.1 and 30.1 g/l, respectively.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180312
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  • 59
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    Electronic Resource
    Bacteria in biology, biotechnology and medicine (fourth edition). Chichester, New York, Weinheim, Brisbane, Singapore, Toronto: John Wiley & Sons, Ltd. 414 pages, 104 figures, 16 photographic plates, 21 tables; £ 45.00, $ 80.00. ISBN 0-471-97468-4 (paperback) (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 287-288 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: No Abstracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180315
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  • 60
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    Studies on whey fermentation using lactic acid bacteria L. acidophilus and L. bulgaricus (1998)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 18 (1998), S. 277-286 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The fermentation process of acid curd whey using pure cultures of L. bulgaricus and L. acidophilus was investigated. The influence of the starter culture amount on the acidification rate in the fermentation was specified, the biological value of fermented and fermented-ammoniated curd whey was determined, and the ability of fermented whey to prevent the injurious effect of Bac. mesenthericus on the wheat bread quality was examined.Acid curd whey was fermented up to a titratable acidity of 19.8-21.6 g lactic acid/kg whey using L. acidophylus and L. bulgaricus. Mathematical equations were developed on the basis of experimental data to calculate the titratable acidity (A) as a functionof fermentation time (τ) and temperature (t). Fermentation and fermentation-ammoniation processes increase the biological value of whey (the content of the vitamins B1, B2, B6, PP and the free amino acids increase). A new dry fodder BIOLAKTS was developed from fermented curd whey and was recommended for use in veterinary medicine. The fermentation-ammoniation process of curd whey was carried out by adding calculated amounts of non-protein nitrogen NH4OH to increase the total protein equivalent and to achieve mutual proportions of protein and lactose 1:1.4, as in skimmed milk. Fermented-ammoniated curd whey was used to obtain a skimmed milk substitute. A dry flour lactic acid concentrate (FLC) was created as a mixture of high quality wheat flour and evaporated fermented whey in established ratios. As our experiments prove, it can be used as an additive in bread-making to prevent the spoiling of wheat bread by Bac. mesenthericus.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370180314
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  • 61
    Electronic Resource
    Electronic Resource
    Masthead (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996) 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320120301
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  • 62
    Electronic Resource
    Electronic Resource
    Current awareness on yeast (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 299-306 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320120302
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  • 63
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    Pyruvate decarboxylase: An indispensable enzyme for growth of Saccharomyces cerevisiae on glucose (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 247-257 
    Details
    ISSN: 0749-503X
    Keywords: pyruvate decarboxylase ; sugar metabolism ; Saccharomyces cerevisiae ; metabolic compartmentation ; acetyl-CoA ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In Saccharomyces cerevisiae, the structural genes PDC1, PDC5 and PDC6 each encode an active pyruvate decarboxylase. Replacement mutations in these genes were introduced in a homothallic wild-type strain, using the dominant marker genes APT1 and Tn5ble. A pyruvate-decarboxylase-negative (Pdc-) mutant lacking all three PDC genes exhibited a three-fold lower growth rate in complex medium with glucose than the isogenic wild-type strain. Growth in batch cultures on complex and defined media with ethanol was not impaired in Pdc- strains. Furthermore, in ethanol-limited chemostat cultures, the biomass yield of Pdc- and wild-type S. cerevisiae were identical. However, Pdc- S. cerevisiae was unable to grow in batch cultures on a defined mineral medium with glucose as the sole carbon source. When aerobic, ethanol-limited chemostat cultures (D = 0·10 h-1) were switched to a feed containing glucose as the sole carbon source, growth ceased after approximately 4 h and, consequently, the cultures washed out. The mutant was, however, able to grow in chemostat cultures on mixtures of glucose and small amounts of ethanol or acetate (5% on a carbon basis). No growth was observed when such cultures were used to inoculate batch cultures on glucose. Furthermore, when the mixed-substrate cultures were switched to a feed containing glucose as the sole carbon source, wash-out occurred. It is concluded that the mitochondrial pyruvate dehydrogenase complex cannot function as the sole source of acetyl-CoA during growth of S. cerevisiae on glucose, neither in batch cultures nor in glucose-limited chemostat cultures.
    Additional Material: 6 Ill.
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  • 64
    Electronic Resource
    Electronic Resource
    Effects of a novel DNA-damaging agent on the budding yeast Saccharomyces cerevisiae cell cycle (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 349-359 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; rad9 ; mutant ; alkylating agents ; cell cycle ; checkpoints ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have investigated the effects on Saccharomyces cerevisiae of a novel antitumour agent (FCE24517 or Tallimustine) which causes selective alkylations to adenines in the minor groove of DNA. Tallimustine, added to wild-type cells for short periods, reduced the growth rate and increased the percentage of budded cells and delayed the cell cycle in the late S+G2+M phases. In the rad9Δ null mutant cells, Tallimustine treatment did not affect growth rate and the percentage of budded cells but greatly reduced cell viability compared to isogenic cells. Consistent with a role of RAD9 in inducing a transient delay in G2 phase which preserves cell viability, the potent cytotoxic effect of the drug on rad9Δ cells was alleviated by treatment with nocodazole. Tallimustine was also found to delay the resumption from G1 arrest of wild-type but not of rad9Δ cells. These data indicate that the effects of Tallimustine on cell cycle progression in yeast are mediated by the RAD9 gene product. From our data it appears that yeast could be a valuable model system to study the mode of action of this alkylating drug and of minor groove alkylators in general.
    Additional Material: 7 Ill.
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  • 65
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    Physical mapping of a centromere-proximal region of chromosome IV-l defines the placement of genes USO1, MBP1, PSA1 and SLC1 (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 411-413 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome IV ; USO1 ; INT1 ; MBP1 ; PSA1 ; SLC1 ; YLA1 ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A physical map of a 14·5 kb region close to the centromere on the left arm of chromosome IV of Saccharomyces cerevisiae is presented. This map has been constructed by restriction analysis of a clone from a YCp50 genomic library and by use of pre-existing and new sequence data from this region. The map reveals the following gene order (reading from the most centromere-distal to the most centromere-proximal locus): USO1/INT1-MBP1-PSA1-SLC1-YLA1 and defines the size of the open reading frames and intergenic regions.
    Additional Material: 1 Ill.
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    Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 391-402 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; gene duplication ; ribosomal protein ; dnaJ homologue ; fork head domain ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A sequence of 31431 bp located on the left arm of chromosome (chr.) XIV from Saccharomyces cerevisiae was analysed. A total of 18 open reading frames (ORFs) could be identified. Twelve ORFs are new, two of which are most likely ribosomal protein genes, leaving ten ORFs of unknown function. Nine of the 18 ORFs show either at least 20% overall amino acid identity or significant regional homology to other S. cerevisiae ORFs. Additionally, six of these nine ORFs have homologues of similar size and the same transcriptional orientation within a stretch of 50 kb on chromosome IX. The degree of homology ranges from 90% overall identity to 23% in 375 amino acids. The homologues on chromosome IX are grouped in two blocks that are separated by relatively long ORFs. This is the first example of a multi-gene duplication in S. cerevisiae not linked to a centromere or subtelomere region. The sequence has been deposited in the EMBL data library under Accession Number X86470.
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    Masthead (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996) 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320120401
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    Genomic reorganization between two sibling yeast species, Saccharomyces bayanus and Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 757-764 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces bayanus ; Saccharomyces cerevisiae ; chromosomal rearrangement ; translocation ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Genomic comparison of two sibling yeast species, Saccharomyces bayanus and Saccharomyces cerevisiae, was performed by Southern blot analysis with various S. cerevisiae gene probes following electrophoretic karyotyping. Fifteen genes on chromosome IV of S. cerevisiae were examined and classified into two groups. Gene probes of CEN4 and TRP1, as well as six other genes located on the left arm of the chromosome hybridized to a 1100-kb chromosome of S. bayanus that is smaller than chromosome IV of S. cerevisiae. On the other hand, probes of seven genes located on the right arm of chromosome IV hybridized to a 1350-kb chromosome that is homeologous to chromosome IV, judging from its size. Two genes located on the left arm of chromosome II hybridized to the 1350-kb chromosome, while four genes on the right arm hybridized to the 1100-kb chromosome. These pieces of evidence indicate that chromosomes II and IV of S. cerevisiae are rearranged into 1350-kb and 1100-kb chromosomes in S. bayanus. Furthermore, it is suggested that chromosome XV is rearranged into two chromosomes (800 and 850 kb in size) in S. bayanus. The translocation points of chromosomes II and IV were delimited using S. cerevisiae prime clone membranes. The results indicated that the translocation points are located close to the FUR4 locus on chromosome II and close to the RAD57 locus on chromosome IV.
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    Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 823-832 
    Details
    ISSN: 0749-503X
    Keywords: aspartyl protease ; proteolytic activation ; zymogen ; yeast ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The vacuolar aspartyl protease proteinase A (PrA) of Saccharomyces cerevisiae is encoded as a preproenzyme by the PEP4 gene and transported to the vacuole via the secretory route. Upon arrival of the proenzyme proPrA to the vacuole, active mature 42 kDa PrA is generated by specific proteolysis involving the vacuolar endoprotease proteinase B (PrB). Vacuolar activation of proPrA can also take place in mutants lacking PrB activity (prb1). Here an active 43 kDa species termed pseudoPrA is formed, probably by an autocatalytic process. When the PEP4 gene is overexpressed in wild-type cells, mature PrA can be found in the growth medium. We have found that prb1 strains overexpressing PEP4 can form pseudoPrA extracellularly. N-terminal amino acid sequence determination of extracellular, as well as vacuolar pseudoPrA showed that it contains nine amino acids of the propeptide, indicating a cleavage between Phe67 and Ser68 of the preproenzyme. This cleavage site is in accordance with the known substrate preference for PrA, supporting the notion that pseudoPrA is formed by autoactivation. When a multicopy PEP4 transformant of a prb1 mutant was grown in the presence of the aspartyl protease inhibitor pepstatin A, a significant level of proPrA was found in the growth medium. Our analyses show that overexpression of PEP4 leads to the secretion of proPrA to the growth medium where the zymogen is converted to pseudoPrA or mature PrA in a manner similar to the vacuolar processing reactions. Amino acid sequencing of secreted proPrA confirmed the predicted cleavage by signal peptidase between Ala22 and Lys23 of the preproenzyme.
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    Identification of ACT4, a novel essential actin-related gene in the yeast Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 839-848 
    Details
    ISSN: 0749-503X
    Keywords: actin-related protein ; DAPI staining ; gene disruption ; chromosome X ; Saccharomyces cerevisiae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Actin molecules are major cytoskeleton components of all eukaryotic cells. All conventional actins that have been identified so far are 374-376 amino acids in size and exhibit at least 70% amino acid sequence identity when compared with one another. In the yeast Saccharomyces cerevisiae, one conventional actin gene ACT1 and three so-called actin-related genes, ACT2, ACT3 and ACT5, have been identified. We report here the discovery of a new actin-related gene in this organism, which we have named ACT4. The deduced protein, Act4, of 449 amino acids, exhibits only 33·4%, 26·7%, 23·4% and 29·2% identity to Act1, Act2, Act3 and Act5, respectively. In contrast, it is 68·4% identical to the product of the Schizosaccharomyces pombe Act2 gene and has a similar level of identity to other Sch. pombe Act2 homologues. This places Act4 in the Arp3 family of actin-related proteins. ACT4 gene disruption and tetrad analysis demonstrate that this gene is essential for the vegetative growth of yeast cells. The act4 mutants exhibit heterogenous morphological phenotypes. We hypothesize that Act4 may have multiple roles in the cell cycle. The sequence has been deposited in the Genome Sequence Data Base under Accession Number L37111.
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    The targeting of bacillus subtilis levansucrase in yeast is correlated to both the hydrophobicity of the signal peptide and the net charge of the N-terminus mature part (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 953-963 
    Details
    ISSN: 0749-503X
    Keywords: Heterologous gene expression ; levansucrase ; signal peptide ; B. subtilis ; S. cerevisiae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We compared the ability of signal sequences from various Bacillus or yeast secreted proteins to direct Bacillus subtilis levansucrase into the secretion pathway of the yeast Saccharomyces cerevisiae. The efficiency of these sequences correlated with the overall hydrophobicity of their h-domain and was independent of their origin. Furthermore, the net charge of the proximal protein sequence downstream from the signal sequence contributed to the competence of the heterologous proteins to be secreted by yeast. Modification of this net charge allowed the protein to be translocated under the control of the yeast invertase signal sequence. Moreover, glycosylation of levansucrase did not modify significantly the fructosyl polymerase activity.
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    Characterization of the SAC3 gene of Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 965-975 
    Details
    ISSN: 0749-503X
    Keywords: act1-1 ; SAC3 ; ConA-labelling ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A temperature-sensitive mutation (act1-1) in the essential actin gene of Saccharomyces cerevisiae can be suppressed by mutations in the SAC3 gene. A DNA fragment containing the SAC3 gene was sequenced. SAC3 codes for a 150 kDa hydrophillic protein which does not show any significant similarities with other proteins in the databases. Sac3 therefore is a novel yeast protein. A nuclear localization of Sac3 is suggested by the presence of a putative nuclear localization signal in the Sac3 sequence. A SAC3 disruption mutation was constructed. SAC3 disruption mutants were viable but grew more slowly and were larger than wild-type cells. In contrast to the sac3-1 mutation, the SAC3 disruption was not able to suppress the temperature sensitivity and the osmosensitivity of the act1-1 mutant. This demonstrates that act1-1 suppression by sac3-1 is not the result of a simple loss of SAC3 function. Furthermore, we examined the act1-1 and the sac3 mutants for defects in polarized cell growth by FITC-Concanavalin A (Con A)-labelling. The sac3 mutants showed a normal ConA-labelling pattern. In the act1-1 mutant, however, upon shift to non-permissive temperature, newly synthesized cell wall material, instead of being directed towards the bud, was deposited at discrete spots in the mother cell.
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    Current awareness on yeast (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 991-998 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121002
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    A computer filtering method to drive out tiny genes from the yeast genomeThis paper is dedicated to the memory of Angelos Kalogeropoulos who left us prematurely. (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1163-1178 
    Details
    ISSN: 0749-503X
    Keywords: Gene prediction ; correspondence analysis ; functional analysis ; Saccharomyces cerevisiae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The authors of the first yeast chromosome sequence defined a minimum threshold requirement of 100 codons, above which an open reading frame (ORF) is retained as a putative coding sequence. However, at least 58 yeast genes shorter than 100 codons have an assigned protein function. Therefore, the yeast genome may contain other tiny but functionally important genes that are discarded from analyses by this simple filtering rule.We have established discriminant functions from the in-phase hexamer frequencies of functional genes and of simulated ORFs derived from a stationary Markov chain model. Fifty-two out of the 58 genes were recognized as coding ORFs by our discriminating method. The test was also applied to all the small ORFs (36 to 100 codons) found in the intergenic regions of published chromosomes. It retained 140 new potential tiny coding sequences, among which we identified seven new genes by similarity searches. Our method, used conjointly with similarity searches, can also highlight sequencing errors resulting from the disruption of the coding frame of longer ORFs. This method, by its ability to detect potential coding ORFs, can be a very useful tool for functional analysis.
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    The S. cerevisiae nitrogen starvation-induced Yvh1p and Ptp2p phosphatases play a role in control of sporulation (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1135-1151 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; sporulation ; phosphatase ; nitrogen metabolism ; gene regulation ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Starvation for nitrogen in the absence of a fermentable carbon source causes diploid Saccharomyces cerevisiae cells to leave vegetative growth, enter meiosis, and sporulate; the former nutritional condition also induces expression of the YVH1 gene that encodes a protein phosphatase. This correlation prompted us to determine whether the Yvh1p phosphatase was a participant in the network that controls the onset of meiosis and sporulation. We found that expression of the IME2 gene, encoding a protein kinase homologue required for meiosis- and sporulation-specific gene expression, is decreased in a yvh1 disrupted strain. We also observed a decrease, albeit a smaller one, in the expression of IME1 which encodes an activator protein required for IME2 expression. Under identical experimental conditions, expression of the MCK1 and IME4 genes (which promote sporulation but do not require Ime1p for expression) was not affected. These results demonstrate the specificity of the yvh1 disruption phenotype. They suggest that decreased steady-state levels of IME1 and IME2 mRNA were not merely the result of non-specific adverse affects on nucleic acid metabolism caused by the yvh1 disruption. Sporulation of a homozygous yvh1 disruption mutant was delayed and less efficient overall compared to an isogenic wild-type strain, a result which correlates with decreased IME1 and IME2 gene expression. We also observed that expression of the PTP2 tyrosine phosphatase gene (a negative regulator of the osmosensing MAP kinase cascade), but not the PTP1 gene (also encoding a tyrosine phosphatase) was induced by nitrogen-starvation. Although disruption of PTP2 alone did not demonstrably affect sporulation or IME2 gene expression, sporulation was decreased more in a yvh1, ptp2 double mutant than in a yvh1 single mutant; it was nearly abolished in the double mutant. These data suggest that the YVH1 and PTP2 encoded phosphatases likely participate in the control network regulating meiosis and sporulation. Expression of YVH1 and PTP2 was not affected by nitrogen source quality (asparagine compared to proline) suggesting that nitrogen starvation-induced YVH1 and PTP2 expression and sensitivity to nitrogen catabolite repression are on two different branches of the nitrogen regulatory network.
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    Masthead (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996) 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121101
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    Current awareness on yeast (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1179-1186 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121102
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    Cloning of Candida albicans SEC14 gene homologue coding for a putative essential function (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1097-1105 
    Details
    ISSN: 0749-503X
    Keywords: SEC14 ; Candida albicans ; protein secretion ; pathogenic fungi ; PI-TP ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The yeast SEC14 gene product is required for the transport of proteins from the Golgi complex. We have cloned the homologous Candida albicans SEC14 gene (CaSEC14) by functional complementation of a Saccharomyces cerevisiae thermosensitive mutant, sec14. Some putative TATA boxes have been identified in CaSEC14 and, contrary to S. cerevisiae SEC14, no introns were found in the Candida homologue. Sequence analysis revealed that CaSec14p is a 301 amino acid protein, 67% identical to S. cerevisiae and Kluyveromyces lactis Sec14p, and 61% identical to the 300 amino-terminal residues of Yarrowia lipolytica Sec14p. Hydrophatic profile analysis of CaSec14p suggests a soluble protein without transmembrane domains, as has been described for the S. cerevisiae counterpart. While it was easy to disrupt one allele of SEC14 in C. albicans, repeated attempts to disrupt the second allele were unsuccessful, thus suggesting that the gene could be essential for vegetative growth in C. albicans. The sequence has been deposited in the EMBL data library under Accession Number X81937.
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    Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1107-1124 
    Details
    ISSN: 0749-503X
    Keywords: HMG-CoA reductase ; endoplasmic reticulum ; molecular evolution ; Schizosaccharomyces pombe ; lovastatin ; karmellae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The synthesis of mevalonate, a molecule required for both sterol and isoprene biosynthesis in eukaryotes, is catalysed by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase. Using a gene dosage approach, we have isolated the gene encoding HMG-CoA reductase, hmg1+, from the fission yeast Schizosaccharomyces pombe (Accession Number L76979). Specifically, hmg1+ was isolated on the basis of its ability to confer resistance to lovastatin, a competitive inhibitor of HMG-CoA reductase. Gene disruption analysis showed that hmg1+ was an essential gene. This result provided evidence that, unlike Saccharomyces cerevisiae, S. pombe contained only a single functional HMG-CoA reductase gene. The presence of a single HMG-CoA reductase gene was confirmed by genomic hybridization analysis. As observed for the S. cerevisiae HMG1p, the hmg1+ protein induced membrane proliferations known as karmellae. A previously undescribed ‘feed-forward’ regulation was observed in which elevated levels of HMG-CoA synthase, the enzyme catalysing the synthesis of the HMG-CoA reductase substrate, induced elevated levels of hmg1+ protein in the cell and conferred partial resistance to lovastatin.The amino acid sequences of yeast and human HMG-CoA reductase were highly divergent in the membrane domains, but were extensively conserved in the catalytic domains. We tested whether the gene duplication that produced the two functional genes in S. cerevisiae occurred before or after S. pombe and S. cerevisiae diverged by comparing the log likelihoods of trees specified by these hypotheses. We found that the tree specifying post-divergence duplication had significantly higher likelihood. Moreover, phylogenetic analyses of available HMG-CoA reductase sequences also suggested that the lineages of S. pombe and S. cerevisiae diverged approximately 420 million years ago but that the duplication event that produced two HMG-CoA reductase genes in the budding yeast occurred only approximately 56 million years ago. To date, S. pombe is the only unicellular eukaryote that has been found to contain a single HMG-CoA reductase gene. Consequently, S. pombe may provide important opportunities to study aspects of the regulation of sterol biosynthesis that have been difficult to address in other organisms and serve as a test organism to identify novel therapies for modulating cholesterol synthesis.
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    RNA-dependent RNA polymerase activity related to the 20S RNA replicon of Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1219-1228 
    Details
    ISSN: 0749-503X
    Keywords: replication ; WdsRNA ; RNA polymerase ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Saccharomyces cerevisiae contains two double-stranded RNA (dsRNA) viruses (L-A and L-BC) and two different single-stranded (ssRNA) replicons (20S RNA and 23S RNA). Replicase (dsRNA synthesis on a ssRNA template) and transcriptase (ssRNA synthesis on a dsRNA template) activities have been described for L-A and L-BC viruses, but not for 20S or 23S RNA. We report the characterization of a new in vitro RNA replicase activity in S. cerevisiae. This activity is detected after partial purification of a particulate fraction in CsCl gradients where it migrates at the density of free protein. The activity does not require the presence of L-A or L-BC viruses or 23S RNA, and its presence or absence is correlated with the presence or absence of the 20S RNA replicon. Strains lacking both this RNA polymerase activity and 20S RNA acquire this activity when they acquire 20S RNA by cytoduction (cytoplasmic mixing). This polymerase activity converts added ssRNA to dsRNA by synthesis of the complementary strand, but has no specificity for the 3′ end or internal template sequence. Although it replicates all tested RNA templates, it has a template size requirement, being unable to replicate templates larger than 1kb. The replicase makes dsRNA from a ssRNA template, but many single-stranded products due to a terminal transferase activity are also formed. These results suggest that, in contrast to the L-A and L-BC RNA polymerases, dissociation of 20S RNA polymerase from its RNA (or perhaps some cellular factor) makes the enzyme change its specificity.
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    SHM1: A multicopy suppressor of a temperature-sensitive null mutation in the HMG1-like abf2 gene (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1239-1250 
    Details
    ISSN: 0749-503X
    Keywords: HM ; ABF2 ; SHM1 ; mitochondrial carrier proteins ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: HM, an HMG1-like mitochondrial DNA-binding protein, is required for maintenance of the yeast mitochondrial genome when cells are grown in glucose. To better understand the role of HM in mitochondria, we have isolated several multicopy suppressors of the temperature-sensitive defect associated with an abf2 null mutation (lacking HM protein). One of these suppressors, SHM1, has been characterized at the molecular level and is described herein. SHM1 encodes a protein (SHM1p) that shares sequence similarity to a family of mitochondrial carrier proteins. On glycerol medium, where mitochondrial function is required for growth, shm1 deletion mutants are able to grow, whereas shm1 abf2 double mutants are severely inhibited. These results suggest that SHM1p plays an accessory role to HM in the mitochondrion. The GenBank Accession Number for the SHM1 sequence is U08352.
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    N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1229-1238 
    Details
    ISSN: 0749-503X
    Keywords: alpha1,2-mannosidase ; calnexin ; endoplasmic reticulum ; degradation ; glycosylation ; yeast ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The endoplasmic reticulum (ER) of eukaryotic cells contains a quality control system, that is required for the proteolytic removal of aberrantly folded proteins that accumulate in this organelle. We used genetic and biochemical methods to analyse the involvement of N-glycosylation in the degradation of a mutant derivative of carboxypeptidase yscY in the ER of the yeast Saccharomyces cerevisiae. Our results demonstrate that N-glycosylation of this protein is required for its degradation since an unglycosylated species is retained stably in the ER. Cells that were devoid of the ER-processing α1,2-mannosidase showed reduced degradation of the glycosylated substrate protein. Disruption of CNE1, a gene encoding a putative yeast homologue for calnexin, did not exhibit any effects on the degradation of this substrate protein in vivo. Also, the α1,2-mannosidase-dependent reduction in the degradation rate did not show any correlation with the function of the CNE1 gene product. Our results suggest that the ER of yeast contains a glycosylation-dependent quality control system, as has been shown for higher eukaryotic cells.
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    Functional conservation of cytosolic proteins required for endosomal vesicle fusion (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1251-1262 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; Sec18 ; endocytosis ; NEM ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recent studies suggest that intracellular membrane traffic relies upon families of related proteins which confer specificity to individual transport reactions but which operate in tandem with a ubiquitous fusogenic complex containing the N-ethylmaleimide-sensitive fusion protein (NSF). The extent to which components of this process are functionally conserved is apparent from the finding that yeast Sec18 protein (Sec18p) can substitute for mammalian NSF in intra-Golgi transport reactions. Here we report that yeast cytosol can support mammalian endosomal vesicle fusion, demonstrating conservation of cytosolic components required for this reaction. Furthermore, under conditions in which the fusion reaction is NSF-dependent we show that yeast Sec18p can functionally substitute for NSF, showing that the yeast protein is capable of catalysing at least two distinct mammalian membrane fusion events. In addition we exploit the complex pattern of sensitivity of the mammalian reaction to N-ethylmaleimide (NEM), coupled with the use of yeast cytosol, to dissect a number of factors required for fusion. We reveal at least three novel NEM-sensitive activities. One of these can be restored by yeast cytosol suggesting that it is functionally conserved.
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    Mapping of gene controlling thiamine transport in Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1279-1283 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; thiamine transport ; recessive allele ; chromosome VII ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A recessive mutation leading to complete loss of thiamine uptake in Saccharomyces cerevisiae was mapped on the left arm of chromosome VII, approximately 56cM centromere-distal to trp5. As the analysed locus is relatively distant from its centromere and from the markers used, its attachment to chromosome VII was confirmed by chromosome loss methods.
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    The sequence of a 23·4kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a ty3 element and 11 new open reading frames (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1273-1277 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; right arm of chromosome VII ; cosmid clone pEGH054 ; CLB6 ; SPT6 ; RP28A ; NUP57 ; Ty element ; autonomous replicating sequence ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DNA sequence of 23427bp from the right arm of chromosome VII of Saccharomyces cerevisiae is reported. The sequence contains 18 open reading frames (ORFs). Four of these are identical to genes already known. G5970 corresponds to the CLB6 gene. G6169 is identical to the SPT6 gene. G6178 represents the RPS28A gene and G6320 corresponds to the 3′-region from the NUP57 gene. Four ORFs (G5978, G5982, G5984, G5995) belong to a Ty3-1 element. A further ORF (G5975) encodes a tRNAcys. The other ORFs revealed no significant similarity to any known gene.The DNA and protein sequences have been deposited in the EMBL Data bank. They are available under the following accession numbers: ORF G 5970, G 5975, G 5978, G 5982, G 5984, G 5995, G 5999, G 6140, G 6145, G 6150, G 6153, G 6163, G 6166, G 6169, G 6172, G 6178, G 6320; DNA sequence accession Z72894/ X70436/ X72890, M34549,  - , Z72895, Z72896, Z72897, Z72898, Z72899, Z72899, Z72899/ M34391, Z72902, Z72903/ M96570, Z72904/ X83099/ X81155; Protein sequence accession S64417/ S43736, S41736,  - , S64417, S64419, S64420, S64421, S64422, S64423, S64423/ A36468, S64425, S64426/ A46703, S64428 /S51799/ S55976.
    Additional Material: 1 Ill.
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  • 86
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    Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1187-1200 
    Details
    ISSN: 0749-503X
    Keywords: dextranase ; Penicillium minioluteum ; Pichia pastoris ; heterologous gene expression ; protein secretion ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DEX gene encoding an extracellular dextranase was isolated from the genomic DNA library of Penicillium minioluteum by hybridization using the dextranase cDNA as a probe. Comparison of the gene and cDNA sequences revealed that the DEX gene does not contain introns. Amino acid sequences comparison of P. minioluteum dextranase with other reported dextranases reveals a significant homology (29% identity) with a dextranase from Arthrobacter sp. CB-8. The DEX gene fragment encoding a mature protein of 574 amino acids was expressed in the methylotrophic yeast Pichia pastoris by using the SUC2 gene signal sequence from Saccharomyces cerevisiae under control of the alcohol oxidase-1 (AOX1) promoter. Over 3·2g/l of enzymatically active dextranase was secreted into the medium after induction by methanol. The yeast product was indistinguishable from the native enzyme in specific activity and the N-terminus of both proteins were identical.
    Additional Material: 8 Ill.
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  • 87
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    Mutations in an Abf1p binding site in the promoter of yeast RPO26 shift the transcription start sites and reduce the level of RPO26 mRNA (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1339-1350 
    Details
    ISSN: 0749-503X
    Keywords: RPO26 ; ABF1 ; transcription initiation ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A binding site for the transcription factor Abf1p was identified as an important promoter element of the gene that encodes Rpo26, a subunit common to all three yeast nuclear RNA polymerases (RNAP). Mutations in the Abf1p binding site were identified among a pool of rpo26 mutant alleles that confer synthetic lethality in combination with a temperature-sensitive mutation (rpo21-4) in the gene that encodes the largest subunit of RNAPII (Rpo21p). In the presence of the wild-type allele of RPO21 these rpo26 promoter mutations confer a cold-sensitive growth defect. Electrophoretic mobility-shift assays using purified Abf1p demonstrated that Abf1p binds to the RPO26 promoter and that the promoter mutations abolish this binding in vitro. Quantitation of the amount of RPO26 mRNA showed that mutations in the Abf1p binding site reduce the expression of RPO26 by approximately 60%. Mutations that affect Abf1p binding also result in a shift of the RPO26 transcriptional start sites to positions further upstream than normal. These results suggest that binding of the Abf1p transcription factor to the RPO26 promoter is important not only in establishing the level of transcription for this gene, but also in positioning the initiation sites of transcription.
    Additional Material: 5 Ill.
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  • 88
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    Current awareness on yeast (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1385-1392 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121302
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  • 89
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    Sequence of a 39 411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1555-1562 
    Details
    ISSN: 0749-503X
    Keywords: chromosome sequencing ; Saccharomyces cerevisiae ; ADH4 ; FZF1 ; HKB ; RTG2 ; HFM1 ; PDE1 ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have sequenced a DNA fragment of 39 411 bp which includes part of the left telomere of chromosome VII of Saccharomyces cerevisiae. We have identified 19 open reading frames (ORFs); six correspond to known yeast genes (ADH4, FZF1, HKB, RTG2, HFM1 and PDE1), nine have similarity with other genes and four exhibit no significant similarity with any known gene. The average size of these ORFs seems to be related to their location, the eight ORFs nearest the telomere being shorter than the 11 others. These two groups of genes are separated by a region of 4·5 kb devoid of significant ORFs. One ORF, NRF120, is a new member of the seripauperine family, represented once in all sequenced yeast chromosomes, in a subtelomeric location. This sequence has been entered in the EMBL data library under accession number X94357.
    Additional Material: 3 Ill.
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  • 90
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    Analysis of a 22 956 bp region on the right arm of Saccharomyces cerevisiae chromosome XV (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1563-1573 
    Details
    ISSN: 0749-503X
    Keywords: genome sequencing ; Saccharomyces cerevisiae ; chromosome XV ; ORFs ; predictable functions ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We present here the sequence analysis of a DNA fragment (cosmid pUOA1258) located on the right arm of chromosome XV. The 22 956 bp sequence reveals 14 open reading frames (ORFs) longer than 300 bp and the 201 bp RPS33 gene. Among the 14 large ORFs, two overlapping frames are likely to be non-expressed and one corresponds to the known GLN4 gene encoding glutaminyl-tRNA synthetase. Two ORFs, O3571 and O3620, encode putative transcriptional regulators with a Zn(2)-Cys(6) DNA binding domain characteristic of members of the GAL4 family. Among the nine remaining ORFs, five (O3568, O3575, O3590, O3615 and O3625) present significant similarity to proteins of unknown function and four (O3580, O3595, O3630 and O3635) lack homology to sequences present in the databases screened. This sequence has been deposited in the GenBank database under Accession Number U55021.
    Additional Material: 6 Ill.
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  • 91
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    Analysis of a 23 kb region on the left arm of yeast chromosome IV (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1587-1592 
    Details
    ISSN: 0749-503X
    Keywords: genome sequencing ; chromosome IV ; Saccharomyces cerevisiae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have determined the complete nucleotide sequence of a 23 kb segment from the left arm of chromosome IV, which is carried by the cosmid 1L10. This sequence contains the 3′ coding region of the STE7 and RET1 (COP1) genes, and 13 complete open reading frames longer than 300 bp, of which ten correspond to putative new genes and three (CLB3, MSH5 and RPC53) have been sequenced previously. The sequence from cosmid 1L10 was obtained entirely by a combined subcloning and walking primer strategy.
    Additional Material: 4 Ill.
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  • 92
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    Sequence and analysis of a 26·9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1575-1586 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome sequencing ; chromosome XV ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have determined the nucleotide sequence of a fragment of chromosome XV of Saccharomyces cerevisiae cloned into cosmid pEOA048. The analysis of the 26 857 bp sequence reveals the presence of 19 open reading frames (ORFs), and of one RNA-coding gene (SNR17A). Six ORFs correspond to previously known genes (MKK1/SSP32, YGE1/GRPE/MGE1, KIN4/KIN31/KIN3, RPL37B, DFR1 and HES1, respectively), all others were discovered in this work.Only five of the new ORFs have significant homologs in public databases, the remaining eight correspond to orphans (two of them are questionable). O5248 is a probable folylpolyglutamate synthetase, having two structural homologs already sequenced in the yeast genome. O5273 shows homology with a yeast protein required for vanadate resistance. O5268 shows homology with putative oxidoreductases of different organisms. O5257 shows homology with the SAS2 protein and another hypothetical protein from yeast. The last one, O5245, shows homology with a putative protein of Caenorhabditis elegans of unknown function. The present sequence corresponds to coordinates 772 331 to 799 187 of the entire chromosome XV sequence which can be retrieved by anonymous ftp (ftp. mips. embnet. org).
    Additional Material: 5 Ill.
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  • 93
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    Masthead (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996) 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121501
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  • 94
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    Current awareness on yeast (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1593-1600 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121502
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  • 95
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    Identification of proteins of the yeast protein map using genetically manipulated strains and peptide-mass fingerprinting (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1519-1533 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces ; yeast protein map ; protein identification ; mass spectrometry ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In this study we used genetically manipulated strains in order to identify polypeptide spots of the protein map of Saccharomyces cerevisiae. Thirty-two novel polypeptide spots were identified using this strategy. They corresponded to the product of 23 different genes. We also explored the possibilities of using peptide-mass fingerprinting for the identification of proteins separated on our gels. According to this strategy, proteins contained in spots are digested with trypsin and the masses of generated peptides are determined by matrix-assisted laser desorption-ionization mass spectrometry (MALDI-MS). The peptide masses are then used to search a yeast protein database for proteins that match the experimental data. Application of this strategy to previously identified polypeptide spots gave evidence of the feasibility of this approach. We also report predictions on the identities of nine unknown spots using MALDI-MS.
    Additional Material: 5 Ill.
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  • 96
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    A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1535-1548 
    Details
    ISSN: 0749-503X
    Keywords: Yarrowia lipolytica ; cell wall ; mycelium ; cDNA ; YWP1 ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector λgt11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is solubilized following partial degradation of β-glucan by Zymolyase digestion. The protein is localized in the outer surface on the tip of the growing mycelial cells and is found partially cryptic in sub-apical locations, suggesting that it participates directly in the mycelial wall architecture.
    Additional Material: 7 Ill.
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  • 97
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    Publisher's note (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1601-1601 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121602
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  • 98
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    Masthead (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996) 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121601
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  • 99
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    List of referees (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1602-1602 
    Details
    ISSN: 0749-503X
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320121603
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  • 100
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    The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1071-1076 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; genome sequencing ; SLA2 ; ZWF1 ; BLH1 ; KEX2 ; SIN4 ; URE2 ; globin ; DnaJ/kw ; zinc-finger ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In this paper is described the DNA sequence of cosmid 14-5 from chromosome XIV of Saccharomyces cerevisiae. The sequence is 38 855 bases long and contains 21 open reading frames (ORFs) plus three internal ORFs. Six ORFs correspond to known yeast genes (SLA2, ZWF1, BLH1, KEX2, SIN4 and URE2); two other ORFs had already been sequenced because they are adjacent to known genes; the remaining 12 ORFs are novel genes. Of these, one ORF (N1142) is particularly interesting since it shows a significant similarity to mammalian globin. Another ORF (N1254) displays two zinc finger motifs as well as a DNAJ motif. The cosmid sequence has been submitted to the EMBL data library under Accession Number Z69381.
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