IMMOBILIZATION OF GLUCOSE-OXIDASE - A COMPARISON OF ENTRAPMENT AND COVALENT BONDING


ARICA M., HASIRCI V.

JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY, vol.58, no.3, pp.287-292, 1993 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 58 Issue: 3
  • Publication Date: 1993
  • Doi Number: 10.1002/jctb.280580313
  • Title of Journal : JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
  • Page Numbers: pp.287-292
  • Keywords: ENTRAPMENT, COVALENT BONDING, PHEMA, GLUCOSE OXIDASE, PROTEASE IMMOBILIZATION, OPERATIONAL STABILITY, CATALASE, REACTOR, BEADS, ACID

Abstract

Glucose oxidase was immobilized onto poly(2-hydroxyethyl methacrylate) (pHEMA) membranes by two methods: by covalent bonding through epichlorohydrin and by entrapment between pHEMA membranes. The highest immobilization efficiency was found to be 17.4% and 93.7% for the covalent bonding and entrapment, respectively. The K(m) values were 5.9 mmol dm-3, 8.8 mmol dm-3 and 12.4 mmol dm-3 for free, bound and entrapped enzyme, respectively. The V(max) values were 0.071 mmol dm-3 min-1, 0.067 mmol dm-3 min-1 and 0.056 mmol dm-3 min-1 for free, bound and entrapped enzyme. When the medium was saturated with oxygen, K(m) was not significantly altered but V(max) was. The optimum pH values for the free, covalently-bound and entrapped enzyme were determined to be 5, 6, and 7, respectively. The optimum temperature was 30-degrees-C for free or covalently-bound enzyme but 35-degrees-C for entrapped enzyme. The deactivation constant for bound enzyme was determined as 1.7 x 10(-4) min-1 and 6.9 x 10(-4) min-1 for the entrapped enzyme.