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  • 1
    Electronic Resource
    Electronic Resource
    The properties of subtilisin, Novo type, immobilized on porous glass (1995)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 15 (1995), S. 123-129 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Studies of the properties of subtilisin, Novo type, immobilized on porous glass with the aid of hexamethylene diisocyanate were carried out. The immobilized proteinase preparation shows optimum activity at a pH value of 10.7 and at a temperature between 60-65°C. It was stable in a wider range of pH and temperature values than the native subtilisin. The KM values for hemoglobin and BAEE were 9.2 × 10-5 [M] and 139 × 10-5 [M], respectively. Under relatively non-aqueous conditions, immobilised subtilisin was able to synthesize phenylacetic acid ethyl ester.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370150117
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Investigations of subtilisin (Novo type) immobilization on cellulose by means of various methods of support activation (1994)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 14 (1994), S. 205-209 
    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 immobilization of subtilisin, Novo type, on WHATMAN cellulose activated by the glutaraldehyde, diisocyanate, diazo-coupling, and S-triazine method, and on a dialdehyde derivative of cellulose has been studied. The best results of proteinase immobilization were achieved when cellulose was activated by hexamethylene diisocyanate. The preparations of a proteolytic activity of 70 PU/g of support and of an esterase activity of 2.3 EU/g of support were obtained with 14% and 38% yield, respectively.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370140215
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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