Peroxidase (POD) activity was measured in peaches, carrots and potatoe
s after blanching treatments at different constant temperatures. Two i
soenzymes exist, one bound and one soluble. The bound form can be conv
erted into the soluble form by a temperature-dependent conversion reac
tion. Both forms are susceptible to heat denaturation. However; the co
nversion precedes the denaturation of the bound form. Neat denaturatio
n of the enzymes could be described using an exponential decay first o
rder reaction). The temperature dependence of all reaction rates could
be described by Arrhenius' law The simultaneous analysis of bound and
soluble POD in peaches explained 96.4% of the observed variance. The
analysis for carrots and potatoes on bound POD alone, yielded a 'perce
ntage variance accounted for' of 94.5 and 70%, respectively. (C) 1998
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