M. Hendriekx is Senior Research Assistant of the Belgian National Fund for Scientific Research (NFSR)
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The influence of water activity on thermal stability of horseradish peroxidase
Article first published online: 29 JUN 2007
DOI: 10.1111/j.1365-2621.1992.tb01175.x
Issue
1365-2621/asset/cover.gif?v=1&s=514334880206bf9323cb13db52b9cf209526d3b0 "International Journal of Food Science & Technology")
International Journal of Food Science & Technology
Volume 27, Issue 1, pages 33–40, February 1992
Additional Information
How to Cite
HENDRICKX, M., SARAIVA, J., LYSSENS, J., OLIVEIRA, J. and TOBBACK, P. (1992), The influence of water activity on thermal stability of horseradish peroxidase. International Journal of Food Science & Technology, 27: 33–40. doi: 10.1111/j.1365-2621.1992.tb01175.x
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M. Hendriekx is Senior Research Assistant of the Belgian National Fund for Scientific Research (NFSR)
Publication History
- Issue published online: 29 JUN 2007
- Article first published online: 29 JUN 2007
- Abstract
- References
- Cited By
Keywords:
- Decimal reduction time;
- z-value;
- enzyme thermal inactivation;
- low moisture stability
Summary
The thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively).