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Kinetic study of a hollow‐fiber enzyme reactor
Author(s) -
Kitano Hiromi,
Yoshijima Shigemi,
Ise Norio
Publication year - 1980
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.260221212
Subject(s) - permeation , enzyme , chemistry , substrate (aquarium) , fiber , urease , michaelis–menten kinetics , membrane , enzyme assay , membrane reactor , immobilized enzyme , activation energy , chromatography , hollow fiber membrane , chemical engineering , biochemistry , organic chemistry , biology , engineering , ecology
Enzymes, such as urease and uricase, were entrapped in three kinds of hollow fibers. The apparent Michaelis–Menten constants K m (app) obtained for these enzyme reactors were always larger than K m of free enzyme because of the permeation resistance of substrate across the hollow‐fiber membrane. K m (app) increased with increasing degree of permeation resistance across the membrane by the increase in enzyme concentration. The half‐life of the entrapped urease in the continuous reaction system was 60–80% of that of free enzyme. Activation energies of hollow‐fiber enzyme reactors were always smaller than that of the free enzyme, because the activation energy of permeation was smaller than that of the enzyme reaction.