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Preparation and kinetic properties of gel entrapped urate oxidase
Author(s) -
Hinberg I.,
O'Driscoll K. F.
Publication year - 1975
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.260171004
Subject(s) - chemistry , urate oxidase , substrate (aquarium) , chromatography , uric acid , enzyme , titration , diffusion , immobilized enzyme , kinetics , nuclear chemistry , organic chemistry , biochemistry , oceanography , physics , quantum mechanics , thermodynamics , geology
Urate oxidase from hog liver (urate: oxygen oxidoreductase, EC 1.7.33) has been entrapped in a crosslinked 2‐hydroxyethyl methacrylate gel with a 47% retention of activity. The kinetic behavior of the gel entrapped enzyme has been studied in a slurried tank reactor using uric acid as substrate. Internal diffusion effects were found to be negligible for particle sizes below 128 μm. A threefold increase in K m (app) was observed for the 128 μm particles and attributed to diffusional effects. The pH activity profile of the gel entrapped enzyme was bell‐shaped at high substrate concentration and could be fitted to a titration curve of two ionizable groups, a basic group having a p K of 7.9 and an acidic group with a p K of 11.0. The gel entrapped enzyme showed excellent stability between pH 6.5 and 10.5.