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  • 1
    Electronic Resource
    Electronic Resource
    Molecular cloning and expression of the xylanase gene from Chainia in Escherichia coli (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 99 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A complete genomic library of Chainia was constructed in coliphage λ vector gt10 and was screened for the xylanase gene using an 18-mer mixed oligonucleotide probe corresponding to a six-amino acid sequence of low molecular mass Chainia xylanase. Inserts from 11 putative clones, showing hybridization with the oligonucleotide probe at medium stringency, were subcloned in pUC8 and screened for xylanase gene expression using anti-xylanase antibodies. The restriction map of the insert (1.4 kb) from one of the four immunopositive clones (PVX8) showing detectable xyalanase activity was constructed. The xylanase activity of PVX8 was not induced by IPTG or xylan. Reorientation of the insert by directional cloning into pUC9 had no effect on the xylanase activity suggesting that an indigenous promoter from Chainia is responsible for the xylanase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05579.x
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  • 2
    Electronic Resource
    Electronic Resource
    A serine alkaline protease from the fungusConidiobolus coronatus with a distinctly different structure than the serine protease subtilisin Carlsberg (1996)
    Springer
    Archives of microbiology 166 (1996), S. 414-417 
    Details
    ISSN: 1432-072X
    Keywords: Conidiobolus coronatus ; Serine proteases ; Subtilisin Carlsberg
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In view of the functional similarities between subtilisin Carlsberg and the alkaline protease fromConidiobolus coronatus, the biochemical and structural properties of the two enzymes were compared. In spite of their similar biochemical properties, e.g., pH optima, heat stability, molecular mass, pI, esterase activity, and inhibition by diisopropyl fluorophosphate and phenylmethlysulfonylfluoride, the proteases were structurally dissimilar as revealed by (1) their amino acid compositions, (2) their inhibition by subtilisin inhibitor, (3) their immunological response to specific anti-Conidiobolus protease antibody, and (4) their tryptic peptide maps. Our results demonstrate that although they are functionally analogous, theConidiobolus protease is structurally distinct from subtilisin Carlsberg. TheConidiobolus protease was also different from other bacterial and animal proteases (e.g. pronase, protease K, trypsin, and chymotrypsin) as evidenced by their lack of response to anti-Conidiobolus protease antibody in double diffusion and in neutralization assays. TheConidiobolus serine protease fails to obey the general rule that proteins with similar functions have similar primary sequences and, thus, are evolutionarily related. Our results strengthen the concept of convergent evolution for serine proteases and provide basis for research in evolutionary relationships among fungal, bacterial, and animal proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01682989
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  • 3
    Electronic Resource
    Electronic Resource
    Development of Chainia as a host for xylanase gene cloning : Evidence for occurrence of a restriction-modification system (1996)
    Springer
    Biotechnology letters 18 (1996), S. 327-332 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Conditions for genetic transformation of the xylanase-negative (X−) strain of Chainia with pIJ 702 were optimized. The growth of Chainia at 30°C for 36 – 40 h and addition of geletin (1%) to the medium resulted in the maximum yield of protoplasts and regeneration efficiency. Poor transformation efficiency of Chainia (X−) protoplasts by native pIJ 702 versus improved efficiency (16 transformants ug−1 of plasmid DNA) by prior heating of protoplasts at 42°C for 10 min suggests the occurrence of a restriction system in Chainia. Increased transformation efficiency by passage of the plasmid through Chainia together with the altered methylation status of the transformant plasmid presents evidence for the existence of an operative modification system in Chainia. Development of thiostrepton resistance and formation of me1amin pigment in Chainia (X−) by transformation with pIJ 702 reveal that genes from Streptomyces can be functionally expressed by Chainia (X−).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00142953
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilisation and reuse of β-glucosidase from Penicillium funiculosum (1983)
    Springer
    Biotechnology letters 5 (1983), S. 75-78 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary β-Glucosidase from Penicillium funiculosum was immobilized on an inexpensive support (polyamide) using glutaraldehyde. The immobilized preparation also possessed activity towards oligocellulose. The kinetic parameters and reuse potential of the immobilized enzyme were studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00132162
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  • 5
    Electronic Resource
    Electronic Resource
    Enhanced stability of cellulase-free xylanase from Chainia sp. (NCL 82.5.1) (1994)
    Springer
    Biotechnology letters 16 (1994), S. 179-182 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Chainia sp. (NCL 82.5.1) produces an extracellular, cellulase-free xylanase. The ready accessibility of the enzyme to cellulose pulp due to its small size and the absence of cellulase are advantageous features. The enzyme is stable at 40°C for 1h and in a pH range of 5–9 at 4°C. Improved stability of the enzyme at higher temperature and pH are desirable. Effect of a variety of compounds was studied to enhance stability. Glycerol, sorbitol, mannitol (10%) or glycine (1M) had marginal effect on thermostability. Addition of Ca+2 or PEG (10mM) increased the half-life of the enzyme at 60°C. Cysteine (10mM) or Tween-80 (1%) showed 70% protection against thermal inactivation. Xylan (3%) offered complete protection against inactivation of the emzyme at 60°C and at pH 9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01021667
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of pretreatment on the hydrolysis of cellulose by Penicillium funiculosum cellulase and recovery of enzyme (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1863-1871 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Penicillium funiculosum produces a complete cellulase which brings about 97% hydrolysis of cotton and has high β-glucosidase, xylanase, laminarinase, and lichenase activities. This article deals with the effect of different pretreatments on the hydrolysis of sugarcane bagasse by P. funiculosum enzymes and the recovery of enzyme from the insoluble residues. Enzymic saccharification of bagasse pretreated with hot 1N NaOH followed by neutralization with HCI and steam treated under pressure (7 kg/cm2) gave 63 and 59% saccharification, respectively, in 48 h. Hemicellulose is not lost in these pretreatments. With a 30% slurry of steam-treated bagasse, a semisolid mass containing 14% sugar was obtained. A 90% recovery of CMCase, β-glucosidase, and filter paper activity from the hydrolysates was obtained under the following conditions: (1) maintaining the ratio of enzyme to substrate high by stepwise addition of substrate, (2) brief grinding of the residual substrate with glass powder, and (3) addition of 0.4% Tween-80 to the eluting buffer. The high recovery of cellulolytic enzymes indicates that the adsorption of these enzymes on cellulose is not irreversible.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250714
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  • 7
    Electronic Resource
    Electronic Resource
    Simultaneous saccharification and fermentation of cellulose to ethanol using Penicillium funiculosum cellulase and free or immobilized Saccharomyces uvarum cellsNCL Communication No.: 3073 (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1679-1684 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: No. Abstract.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250623
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  • 8
    Electronic Resource
    Electronic Resource
    A rapid and simplified procedure for purification of a cellulase from Fusarium liniThis is NCL communication No. 3067. (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 41-45 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An endo-β-1,4-glucanase (EC 3.2.1.4) was obtained in high yields in purified form a culture filtrate of Fusarium lini by an extremely simple method. The method consists of precipitation of the culture filtrate with ammonium sulphate (290 g/L), followed by chromatography of the precipitated fraction on Biogel P-150. The purification is based on the unusual property of the enzyme being eluted after cytochrome C, even though it molecular weight is 2.8 × 104 (by SDS PAGE). The yield of pure enzyme was 6.8 mg/L culture broth. The homogeneity of the enzyme was established by ultracentrifugation, isoelectric focusing, and electrophoresis in polyacrylamide gels containing SDS. The enzyme was isoelectric at pH 8.3 and contained 2.9% carbohydrate. The Km value for carboxymethyl (CM) cellulose was 11.6 mg/mL. The enzyme showed high viscosity reducing activity towards CM cellulose but very low activity with Walseth cellulose and crystalline celluloses such as Avicel and cotton. The purified enzyme has activity towards xylan. The amino acid analysis showed a predominance of acidic and neutral amino acids and low contents of histidine, arginine, and methionine. One-half of the cysteine content was 11 residues/mol enzyme, and no free-SH group was detectable.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260109
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  • 9
    Electronic Resource
    Electronic Resource
    Mode of action and properties of xylanase and β-Xylosidase from Neurospora crassaNCL Communications No. 3772. (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1832-1837 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Extracellular β-xylosidase (1,4-β-D-xylan xylohydrolase, EC 3.2.1.37) from culture filtrates of Neurospora crassa was purified to homogeneity by preparative isoelectric focusing followed by gel electrophoresis. The molecular weight of the purified xylosidase was 83,000 D and the Km on p-nitrophenyl-β-D-xyloside was 0.047mM. The homogeneous xylanase (1,4-β-D-xylan xylanohydrolase, EC 3.2.1.8) and β-xylosidase showed differences in their mode of action towards xylooligosaccharides. The degree of hydrolysis of D-xylan by xylanase of N. crassa was 18%. Supplementation of β-xylosidase from the same organism resulted in 48% hydrolysis. The synergistic effect was more pronounced, with the hydrolysis of 68%, when a homogeneous preparation of β-xylosidase from Sclerotium rolfsii was added to the saccharification system.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260281210
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  • 10
    Electronic Resource
    Electronic Resource
    Purification, characterization, and synergistic action of endoglucanases from Fusarium liniNCL, Communication No. 3755. (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1100-1105 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Five endoglucanases (1,4-β-D-glucan-glucanohydrolase, EC 3.2.1.4) were isolated from Fusarium lini. Endo I and II were purified by preparative gel electrophoresis and Endo III, IV, and V were purified in a single-step procedure involving preparative flat-bed isoelectric focusing. All the endoglucanases were homogenous on disk gel electrophoresis and analytical isoelectric focusing in polyacrylamide gel. The pi values were between 6 and 6.6 for Endo III, IV, and V; for Endo I, the pi value was 8. The molecular weights of the enzymes were between 4 × 104 and 6.5 × 104. The Km values for endoglucanases using carboxymethyl cellulose (CM-cellulose) as the substrate were 2-12 mg/mL. The specificity of the enzymes was restricted to β-1, 4-linkages. All the enzymes showed activity towards D-xylan. The endoglucanases had high viscosity reducing activity with CM-cellulose. Striking synergism was observed for the hydrolysis of CM-cellulose by endoglucanases. Endo II, IV, and V attacked cellopentaose and cellotetraose more readily than cellotriose. Endo II and V hydrolyzed cellotriose, cellotetraose, and cellopentaose, yielding a mixture of cellobiose with a trace amount of glucose; endo IV produced only cellobiose.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280722
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