ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1962.tb00069.x
Permalink