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  • Chemistry  (4)
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  • 1
    Electronic Resource
    Electronic Resource
    Production of single cell protein from ethanol by fed-batch processOriginally reported at the Second CIS-ACS Joint Conference, in Montreal, Canada, May 29-June 2, 1977. (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1221-1237 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The production of single cell protein (SCP) form ethanol is an interesting process to study from a biochemical engineering viewpoint. The cellular yield mainly depends upon the metabolic activity of the cells and the amount of substrate available. Fedbatch fermentations Were run in a 70 liter highly instrumented computer-coupled fermentor using Candida utilis. Respiratory quotient and culture fluorescence, measuring NADH, indicate by which pathway ethanol is utilized. By monitoring these parameters it is possible to control the ethanol concentration so that accumulation of acetate is minimized and the conversion of ethanol to cell mass is maximized.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210711
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  • 2
    Electronic Resource
    Electronic Resource
    Mixing times and glucose uptake measured with a fluorometer (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1487-1492 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260200915
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  • 3
    Electronic Resource
    Electronic Resource
    Kinetic characterization of the extracellular xylanases of Thermomonospora sp. (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 832-836 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study deals with characterizing the extracellular xylanases produced by a strain of the thermophilic bacterial genus Thermomonospora. Supernatant from centrifuged fermentation broth was used as a crude enzyme preparation. From pH 5.5 to pH 7.7 the temperature optimum based on a 10-min assay of activity was 80°C. The crude enzyme had a half-life of approximately 1 month when stored at 55°C at pH 6.5. The enzyme produced a mixture of xylose oligomers from xylan, with xylobiose occuring in greatest quantity on a molar basis. Only trace quantities of xylose were produced by this hydrolysis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270612
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  • 4
    Electronic Resource
    Electronic Resource
    The β-xylosidase of Thermomonospora (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 909-913 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study is concerned with characterizing cell-bound inducible β-xylosidase produced by a strain of the thermophilic bacterial genus Thermomonospora. A crude preparation of this enzyme recovered from sonicated cells of this organism displayed high activity against paranitrophenyl-β-xylopyranoside over a pH range of 5.5-7.7. The temperature optimum, based on a 30-min assay of activity, at pH 6.5 was 70°C. The crude enzyme had a thermal half-life of approximately 1 week at 55°C and pH 6.5. Xylose inhibited the enzyme. Values of Km and Vmax are estimated from the reaction rate data as 0.82 mM and 8 U/L, respectively.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270626
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