Gel entrapment of enzymes: Kinetic studies of immobilized glucose oxidase | Zendy

Hinberg I. | Zendy; Kapoulas A. | Zendy; Korus R. | Zendy; O'Driscoll K. | Zendy

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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.

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