Characterization of phenol oxidase in a pseudophyllidean cestode Penetrocephalus ganapatii

Abstract

The biochemical characteristics of phenol oxidase obtained from Penetrocephalus ganapatii have been investigated using manometric and electrophoretic techniques. Phenol oxidase was found to have maximum activity at pH 7·4, the Michaelis constant for dopamine was 189 μM and the enzyme was stable between 20 and 40°C. Potassium cyanide, sodium diethyldithiocarbamate and phenylthiourea strongly suppressed enzyme activity. The Ki values for potassium cyanide, diethyldithiocarbamate and phenylthiourea were 33μM, 700 μM and 938 μM respectively. The properties of soluble and insoluble enzymes to various phenolic substrates are discussed.