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Immobilization of glucose oxidase on macroreticular ion exchange resins

Immobilization of glucose oxidase on macroreticular ion exchange resins MATERIALS AND METHODS The glucose oxidase was purchased from Boehringer Mannheim Corp., N. Y., and had a specific activity of 210 enzyme units (EU)/mg. The peroxidase used in the determination of the activity of the soluble glucose oxidase was also purchased from Boehringer and had an activity of 60 EU/mg. The o-dianisidine dye used in the colorimetric methods for glucose oxidase activity was purchased from Sigma Chemical Co., St. Louis, Mo. The macroreticular ion exchange resins were supplied by Rohm and Haas Co., Philadelphia, Penn. Immobilization Procedure The glucose oxidase was dissolved in phosphate buffer which was at the desired pH, usually 5.8. The ion exchange resin was then added to the enzyme solution and the mixture was placed in a shaker bath for at least 3 hr. The amount of enzyme on the resin was taken to be the difference between the initial and final glucose oxidase concentration in the liquid. By varying the initial glucose oxidase concentration of the solution and the amount of resin added, immobilized supports were generated having various enzyme surface densities. Assay Procedures The soluble enzyme concentration was measured by the o-dianisidine dye method which uses the peroxidase enzyme to utilize the http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology and Bioengineering Wiley

Immobilization of glucose oxidase on macroreticular ion exchange resins

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References (7)

Publisher
Wiley
Copyright
Copyright © 1978 John Wiley & Sons, Inc.
ISSN
0006-3592
eISSN
1097-0290
DOI
10.1002/bit.260200413
Publisher site
See Article on Publisher Site

Abstract

MATERIALS AND METHODS The glucose oxidase was purchased from Boehringer Mannheim Corp., N. Y., and had a specific activity of 210 enzyme units (EU)/mg. The peroxidase used in the determination of the activity of the soluble glucose oxidase was also purchased from Boehringer and had an activity of 60 EU/mg. The o-dianisidine dye used in the colorimetric methods for glucose oxidase activity was purchased from Sigma Chemical Co., St. Louis, Mo. The macroreticular ion exchange resins were supplied by Rohm and Haas Co., Philadelphia, Penn. Immobilization Procedure The glucose oxidase was dissolved in phosphate buffer which was at the desired pH, usually 5.8. The ion exchange resin was then added to the enzyme solution and the mixture was placed in a shaker bath for at least 3 hr. The amount of enzyme on the resin was taken to be the difference between the initial and final glucose oxidase concentration in the liquid. By varying the initial glucose oxidase concentration of the solution and the amount of resin added, immobilized supports were generated having various enzyme surface densities. Assay Procedures The soluble enzyme concentration was measured by the o-dianisidine dye method which uses the peroxidase enzyme to utilize the

Journal

Biotechnology and Bioengineering – Wiley

Published: Apr 1, 1978

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