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Cotton cellulose: Enzyme adsorption and enzymatic hydrolysis
Author(s) -
Beltrame P. L.,
Carniti P.,
Focher B.,
Marzetti A.,
Cattaneo M.
Publication year - 1982
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1982.070270925
Subject(s) - adsorption , hydrolysis , trichoderma viride , michaelis–menten kinetics , cellulase , cellulose , langmuir , chemistry , enzymatic hydrolysis , substrate (aquarium) , langmuir adsorption model , enzyme , saturation (graph theory) , chromatography , organic chemistry , polymer chemistry , nuclear chemistry , enzyme assay , biology , ecology , food science , mathematics , combinatorics
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 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.