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Gel entrapment of enzymes: Kinetic studies of immobilized glucose oxidase
Author(s) -
Hinberg I.,
Kapoulas A.,
Korus R.,
O'Driscoll K.
Publication year - 1974
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.260160202
Subject(s) - glucose oxidase , chemistry , enzyme , aspergillus niger , immobilized enzyme , thermal stability , entrapment , chromatography , biochemistry , oxidase test , organic chemistry , medicine , surgery
Glucose oxidase (EC 1.1.3.4, from Aspergillus niger ) has been entrapped in a crosslinked 2‐hydroxycthyl methaerylate gel containing 20% poly(vinyl pyrrolidone). The kinetic behavior and thermal stability of the entrapped enzyme were found to closely approximate that of the free enzyme. The entrapped glucose oxidase shows a broadened pH profile which is attributed to a buffering effect of the gel. Stability of gel entrapped glucose oxidase is extremely good at room temperature, suggesting a variety ofanalytical and control uses for this system.