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 2–8°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 Km, 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.
Cotton Cellulose: Enzyme Adsorption and Enzymatic Hydrolysis / P.L. Beltrame, P. Carniti, B. Focher, A. Marzetti, M. Cattaneo. - In: JOURNAL OF APPLIED POLYMER SCIENCE. - ISSN 0021-8995. - 27:9(1982), pp. 3493-3502.
Cotton Cellulose: Enzyme Adsorption and Enzymatic Hydrolysis
P. CarnitiSecondo
;
1982
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 2–8°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 Km, 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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