Kinetic Studies on the Heat Inactivation of Peroxidase in Sweet Corna
- 1 March 1962
- journal article
- research article
- Published by Wiley in Journal of Food Science
- Vol. 27 (2) , 113-119
- https://doi.org/10.1111/j.1365-2621.1962.tb00069.x
Abstract
SUMMARY: A kinetic procedure employing D values was used instead of the usual end‐point method to study heat inactivation of peroxidase in whole‐kernel sweet corn. Results at 150–200°F indicated that a heat‐labile fraction and a heat‐stable fraction were being inactivated. The resistant fraction represented 5% of total enzyme activity, and was concentrated in the pericarp. Increasing the blanch time at 200°F from 2 to 5 min decreased residual enzyme activity from 3.3% to 1.7%.Inactivation of the heat‐resistant fraction at 210–290°F also followed a first‐order reaction. The phantom inactivation‐time curve showed that an HTST process based on microbial destruction could leave residual enzyme activity.This publication has 5 references indexed in Scilit:
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