Thermostability of Soluble and Immobilized Horseradish Peroxidase

  1. ZHIJUN WENG,
  2. M. HENDRICKX,
  3. G. MAESMANS,
  4. K. GEBRUERS,
  5. P. TOBBACK

Article first published online: 25 AUG 2006

DOI: 10.1111/j.1365-2621.1991.tb05328.x

Issue

Journal of Food Science

Journal of Food Science

Volume 56, Issue 2, pages 574–578, March 1991

Additional Information

How to Cite

WENG, Z., HENDRICKX, M., MAESMANS, G., GEBRUERS, K. and TOBBACK, P. (1991), Thermostability of Soluble and Immobilized Horseradish Peroxidase. Journal of Food Science, 56: 574–578. doi: 10.1111/j.1365-2621.1991.tb05328.x

Author Information

  1. The authors are with the Laboratory of Food Technology, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, 3001 Heverlee, Belgium. Dr. M. Hendrickx is Senior Research Assistant of the National Fund for Scientific Research (Belgium).

Publication History

  1. Issue published online: 25 AUG 2006
  2. Article first published online: 25 AUG 2006
  3. Ms received 1/29/90; revised 5/24/90; accepted 7/22/90

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ABSTRACT

Thermal inactivation kinetics of soluble horseradish peroxidase and the enzyme covalently immobilized onto glass beads were studied in phosphate buffer and organic solvents in a temperature range of 65° to 98°C. The z value of the heat-stable fraction of peroxidase was changed from 26.3°C to 14.1°C by the method of enzyme immobilization. Further, the z value of 14.1°C of the immobilized peroxidase was lowered to 11.1°C using an organic solvent in order to modify the environment of the enzyme.

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