Gel entrapment of enzymes: Kinetic studies of immobilized glucose oxidase

Abstract

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.