Abstract
SummarySoluble and ionically bound peroxidases have been obtained from homogenized Ohane grapes. The soluble fraction contained the highest level of peroxidase activity and accounted for approximately 87% of the total enzymic activity. Plots of the percentage of heat inactivation for the grape peroxidases against time were non‐linear with approximately 90% of the peroxidase activity being destroyed after 10 min at 80°C. Following heat inactivation there was no significant regeneration of enzymic activity. Using isoelectric focusing six isoperoxidases with isoelectric points ranging from approximately pI 3.5 to 9.8 were detected.
Published Version
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