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Cotton cellulose: Enzyme adsorption and enzymatic hydrolysis

✍ Scribed by P. L. Beltrame; P. Carniti; B. Focher; A. Marzetti; M. Cattaneo


Publisher
John Wiley and Sons
Year
1982
Tongue
English
Weight
542 KB
Volume
27
Category
Article
ISSN
0021-8995

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✦ Synopsis


Abstract

Adsorption of a crude cellulase complex from Trichoderma viride on variously pretreated cotton celluloses has been studied in the framework of the Langmuir approach, in the temperature range 2–8Β°C. The saturation amount of adsorbed enzyme has been related to their susceptibility to hydrolysis. In every case the adsorption process was found to be faster by 2–3 orders of magnitude than the hydrolysis step to give end products. For one substrate, the Langmuir parameters were found to be fairly well correlated with the value of the Michaelis constant K~m~, measured for its enzymatic hydrolysis, and the adsorptive complex (ES)~ad~ was indistinguishable from the complex (ES) of the Michaelis–Menten model for the hydrolysis.


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