Characterization of phenoloxidase of Penaeus indicus

Anil Kumar, P and Sridhar, N (1993) Characterization of phenoloxidase of Penaeus indicus. Indian Journal of Fisheries, 40 (4). pp. 251-255.


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The enzyme phenoloxidase from haemolymph of Penaeus indicus was partially purified us- ing ammonium sulphate fractionation technique. An overall recovery of 52% with a 5-fold purification was achieved. Dialysis reduced the enzyme activity indicating the presence of dialysable cofactors. The enzyme had high afinity for the biphenolic substrate adrenalin fol- lowed by dopamine, catechol and dopa. The rate of the reaction was linear up to 3 min when adrenalin was used as the substrate. The enzyme had an optimum tem erature of 50°C but lost 60% of its activity when heated to 70°C for 10 min. The Krn and t"max of the enzyme with adrenalin as the substrate was 0.122 mM and 0.588 OD unitslmg protein a min respectively. The enzyme was inhibited by the substrate adrenalin at a concentration of IS mM and by cupric salts. Magnesium and calcium stimulated the enzyme activity. EDTA and mercaptoethanol strongly inhibited the enzyme.

Item Type: Article
Uncontrolled Keywords: Phenoloxidase; Penaeus indicus
Subjects: Fish Biotechnology
Crustacean Fisheries > Prawn and Prawn fisheries
Divisions: CMFRI-Cochin > Physiology and Nutrition Pathology
Subject Areas > CMFRI Brochures > CMFRI-Cochin > Physiology and Nutrition Pathology
Depositing User: Users 5 not found.
Date Deposited: 11 May 2010 08:50
Last Modified: 09 Sep 2015 15:07

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