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Abstract
SummarySoluble and ionically‐bound peroxidases have been obtained from the pulp and peel of Conference pears. The peel soluble fraction contained the highest level of peroxidase activity. The peel peroxidases, both soluble and ionically bound, were particularly heat stable. Following heat inactivation, regeneration of enzymic activity was observed for the peel peroxidases and soluble pulp enzymes. Plots of the percentage of heat inactivation for the pear peroxidases against heating time were non‐linear.
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