FUW TRENDS IN SCIENCE & TECHNOLOGY JOURNAL
(A Peer Review Journal)
e–ISSN: 2408–5162; p–ISSN: 2048–5170
keywords: Enzyme, inactivation, ripe pawpaw, peroxidase, pH, temperature.
Crude peroxidase (POD) was extracted from ripe pawpaw (Carica papaya) fruit pulp and the enzyme kinetics, activity at varying pH and temperature conditions were studied. The enzyme exhibited maximum activity at pH 7.0 at 10-20oC. The enzyme lost 60% activity at 70oC. The POD had reaction constant (Km) of 0.113M and a maximum catalysis rate (Vmax) of 0.013 enzyme units/g fruit pulp. The enzyme was completely inactivated when incubated at 90oC. The result of the study suggested that crude peroxidase from ripe pawpaw fruit pulp was stable over wide temperature ranges. The value of Km suggests that POD from ripe Carica papaya fruit pulp can be isolated, purified and characterized
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