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Immobilization of enzymes on activated carbon: Properties of immobilized glucoamylase, glucose oxidase, and gluconolactonase
Author(s) -
Cho Y. K.,
Bailey J. E.
Publication year - 1978
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260201011
Subject(s) - glucose oxidase , chemistry , substrate (aquarium) , enzyme , immobilized enzyme , kinetics , adsorption , michaelis–menten kinetics , enzyme kinetics , chromatography , enzyme assay , product inhibition , biochemistry , organic chemistry , non competitive inhibition , active site , biology , ecology , physics , quantum mechanics
Apparent kinetics and pH–activity relationships have been determined for glucoamylase and glucose oxidase immobilized on activated carbon using a diimide method. Reaction rate expressions of Michaelis–Menten form adequately approximate the observed kinetics for both enzyme preparations over the ranges of substrate concentrations considered. Influences of external mass transfer as well as substrate and product adsorption on interpretation of the experimental data have been examined. Immobilization of a glucose oxidase–gluconolactonase enzyme mixture has been found to increase substantially the ratio of gluconolactonase to glucose oxidase activities compared to the corresponding activity ratio for these enzymes in solution.