Gel entrapment of enzymes: Kinetic studies of immobilized glucose oxidase

ADS

Abstract

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.


Publication:

Biotechnology and Bioengineering

Pub Date:
February 1974
DOI:

10.1002/bit.260160202

Bibcode:
1974BiotB..16..159H