Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 2015-2019
  • 1990-1994  (7)
  • 1985-1989  (6)
  • 1960-1964
  • 1930-1934
  • 1925-1929
  • 1905-1909
  • 1850-1859
  • 1840-1849
  • 1830-1839
  • Biochemistry and Biotechnology  (13)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 962-968 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An artisanal static process for protein enrichment of cassava by solid-state fermentation, developed in laboratory and tested on pilot units in Burundi (Central Africa), provides enriched cassava containing 10.7% of dry matter protein versus 1% before fermentation. Cassava chips, processed into granules of 2-4-mm diameter, are moistened (40% water content) and steamed. After cooling to 40°C, cassava is mixed with a nutritive solution containing the inoculum (Rhizopus oryzae, strain MUCL 28627) and providing the following per 100 g dry matter: 3.4 g urea, 1.5 g KH2PO4, 0.8 g MgSO4·7H2O, and 22.7 g citric acid. For the fermentation, cassava, with ca. 60% moisture content, is spread in a thin layer (2-3 cm thick) on perforated trays and slid into an aerated humidified enclosure. The incubation lasts ± 65 h. The production of protein enriched cassava is 3.26 kg dry matter/m2 tray. The effects of the variation of the nutritive solution composition and the inoculum conservation period on the protein production are equally discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 183-186 
    ISSN: 0006-3592
    Keywords: Gluconobacter oxydans ; 5-ketogluconic acid ; tartatic acid ; vanadate ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The dependence of tartaric acid production by Gluconobacter oxydans ssp. oxydans ATCC 19357 and G. oxydans ssp. suboxydans ATCC 621 on vanadate was investigated. It was found with both organisms that trataric acid could only be produced in a medium containing vanadate (NH4VO3). A proposed intermediate of the tartaric acid metabolism in G. oxydans, 5-ketogluconic acid, was tested on its reactivity in the presence of the oxidizing catalyst vanadate. It could be shown that 5-ketogluconic acid and the catalyst vanadate, but not the activity of G. oxydans, were responsible for the formation of tartaric acid. G. oxydans was not able to produce tartaric acid by itself. The stereochemical identity of the formed tartaric acid could be identified as the L-(+)-type. Oxalic acid was formed from 5-ketogluconic acid with vanadate in the absence and in the presence of G. oxydans. The ratio of oxalic acid to tartaric acid was 1:1.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 50-66 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Using the available information of fermentation biochemistry, fermentation (stoichiometric) equations are derived for anaerobic saccharolytic fermentations of butanediol and mixed acids. The equations describe the interrelations among the fermentation products, biomass, and consumed substrate (glucose). The validity of the equations is tested using a variety of batch data from the literature. The validity of the equations is expected to extend to steady-state and transient fermentations, as well. Uses, improvements, and extensions of the equations are also discussed in detail. Among others, it is shown that the equations are useful for checking the consistency of experimental data, for calculating maximal yields and selectivities for the fermentation products, and calculating the extent of utilization of the Embden-Meyerhof-Parnas pathway versus the Hexose Monophosphate pathway of glucose utilization.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 67-80 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Fermentation (stoichiometric) equations are derived for anaerobic fermentations of propionic-acid bacteria (of both the Propionibacterium and acrylate pathways) and for production of various oxychemicals (butanol, acetone, isopropanol, butanediol, butyrate, acetate, propionate, succinate, lactate, and acrylate) from pentoses, hexoses, and cellobiose. The derivations of the equations are based on the fermentation biochemistries of the various bacterial classes. The validity of the equations is tested using fermentation data from the literature. The equations are shown to be valuable, among other uses, for calculating maximal yields and selectivities of the various fermentation products, as “gateway sensors” for monitoring of the fermentations, and for calculating the extents of the various intracellular reactions of the fermentation biochemistry.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1246-1257 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A fermentation system has been designed to demonstrate the use of gas chromatography (GC) for on-line monitoring of the butanol-acetone and other complex saccharolytic fermentations. Tangential flow ultrafiltration was used to sterilely and continuously obtain a cell-free filtrate from the fermentation broth for on-line GC analysis of butanol, butyrate, acetate, acetone, ethanol, and acetoin. The liquid injection system consists of a phosphoric acid contactor, a slider-type injection valve, and a heater to address the difficulties (ghosting) encountered in the analysis of carboxylic acids. The fermentation headspace gas was also analyzed by on-line GC for nitrogen and carbon dioxide, while hydrogen was measured by difference. Raw chromatographic data were analyzed by a chromatography data system. Both raw and processed data were transmitted to a VAX 11/750 computer for further processing (using the fermentation equation) and archiving. The fermentation equation, which has recently been derived and tested on completed fermentation data, was also found to be valid during transient fermentations and thus useful as a gateway sensor for calculating various fermentation parameters on-line. Such parameters include glucose concentration and gas composition, as well as a number of unobservable parameters (such as YATP, excess ATP, and NAD reduced by FdH2), which characterize the state of the fermentation.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 353-358 
    ISSN: 0006-3592
    Keywords: Bagasse hemicellulose hydrolysate ; chemostat ; Candida blankii ; D-xylose ; single cell protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A Candida blankii yeast isolate was grown in sugar cane bagasse hemicellulose hydrolysate at 38°C in carbon-limited chemostat culture. The pretreatment of the acid hydrolysate prior to microbial cultivation consisted of partial neutralization with ammonia and sodium hydroxide, plus the addition of phosphorus, which was the only other growth-limiting nutrient apart from nitrogen. The cell yield coefficient on nitrogen was 16.78. The critical dilution rate was higher (0.35 h-1) in diluted hydrolysate than in undiluted hydrolysate (0.21 h-1). In undiluted hydrolysate at a dilution rate of 0.1 h-1 and pH 4, where aseptic procedures proved unnecessary, the cell and protein yield coefficients were 0.53 and 0.26, respectively, and no residual carbon substrates (D-xylose, L-arabinose, D-glucose, and acetic acid) were detected. The cell yield on oxygen increased linearly as a function of dilution rate. The cellular content of protein, carbohydrate, and RNA also increased with an increase in dilution rate, whereas the DNA content decreased slightly. C. blankii has considerable potential for the production of single cell protein from hemicellulose hydrolysate, because of its ability to utilize all of the major carbon substrates in the hydrolysate at a low pH and at a relatively high temperature with a high protein yield. © 1992 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 760-767 
    ISSN: 0006-3592
    Keywords: (R)-1-(1-naphthyl)ethylamine ; (R)-1-aminoindan ; subtilisin ; organic solvent ; stereoselective aminolysis ; immobilized enzyme ; continuous process ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An enzymatic process has been developed for the continuous production of the pharmaceutically important intermediate (R)-1-aminoindan and of the chiral resolving agent (R)-1-(1-naphthyl)ethylamine. The process consists of the subtilisin catalyzed stereoselective aminolysis of the racemic primary amine with an active ester in organic solvent. The competing nonenzymatic reaction has been suppressed by appropriate choice of solvent and reactant's concentration and by minimizing the time of contact between the amine and the active ester. Subtilisin was immobilized on glass beads and the reaction carried out in a continuous-flow column bioreactor. By using a 450-mL column bioreactor containing 5.7 g of subtilisin immobilized on 570 g of glass beads, 1.6 kg of racemic 1-(1-naphthyl)ethylamine was resolved after 320 h of continuous operation with only a slight loss of the enzymatic activity. During the whole process, the optical purity of the chiral amine eluting from the column was higher than 90%. A facile procedure was developed for separating the unreacted (R)-amine from the (S)-amide and for the recycling of the solvent 3-methyl-3-pentanol and the active ester 2,2,2-trifluoroethyl butyrate. © 1992 John Wiley & Sons, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 4 (1986), S. 123-130 
    ISSN: 0263-6484
    Keywords: Fasting ; pancreatic islets ; insulin release ; 45Ca and 86Rb fluxes ; glucose ; 2-ketoisocaproate ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In pancreatic islets removed from 48 h-fasted rats, as distinct from fed animals, the release of insulin evoked by D-glucose is more severely impaired than that evoked by 2-ketoisocaproate. This decreased secretory response to D-glucose contrasts with an unimpaired cationic response to the sugar in terms of the glucose-induced decrease in both 86Rb and 45Ca outflow from pre-labelled islets. Likewise, fasting only causes a modest decrease of the secondary rise in 45Ca outflow evoked by D-glucose in islets perifused at normal Ca2+ concentration. The latter decrease appears more marked, however, if the cationic response to glucose is expressed relative to that evoked by 2-ketoisocaproate in islets removed from rats in the same nutritional state. It is concluded that, in the process of nutrient-stimulated insulin release, neither the decrease in K+ conductance (inhibition of 86Rb outflow) nor the sequestration of Ca2+ by intracellular organelles and/or direct inhibition of Ca2+ outward transport (decrease in 45Ca outflow) represent the sole determinant(s) of the subsequent gating of Ca2+ channels (secondary rise in 45Ca efflux).
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 11 (1990), S. 510-513 
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Proteins of dog bronchoalveolar lavage fluid, obtained by washing the epithelial lining layer of lungs with phosphate-buffered saline, were separated by two-dimensional electrophoresis. Due to the low protein and high salt content of the bronchoalveolar lavage fluid, samples had to be concentrated and desalted. Following electrophoresis the protein spots were visualized by silver staining. Comparing the two-dimensional protein patterns of bronchoalveolar lavage fluid with that from serum, several lungspecific proteins were detected. The most prominent protein, most probably a surfactant-associated protein, showed isoforms with isoelectric points in the range of pH 4.2-4.8, and a molecular mass of 32 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis after reduction with dithiothreitol.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Preparative continuous free flow-isoelectric focusing has been used to separate at least three different components of intrinsic peptidyl-prolyl cis/trans isomerase (PPIase) activity from erythrocytes lysate. By adding chemical spacer molecules like glycine and Bicine to commercial carrier ampholyte mixtures the resulting pH profile was predictably influenced. With an applied field strength of 125-170 V/cm a residence time of less than 15 min was sufficient for the separation of PPIases with isoelectric points of 5.4, 5.7 and 5.9 from the bulky hemoglobin. The recovery of the overall PPIase activities was about 100%. The purification factor has been determined as 20- to 100-fold. For each isoform of the enzyme the peptidyl-prolyl cis/trans isomerase acitivity of the separated proteins was inhibited by cyclosporin A but was resistant toward FK 506.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...