Properties of phenol oxidase inFasciola gigantica

Abstract

SummaryPhenol oxidase ofFasciola giganticaexists both as the soluble form as well as the membrane-bound form. The membrane-bound enzyme is considered to be a tyrosinase type because it is capable of oxidizing mono- and diphenol and is inefficient in oxidizing paraphenols. The soluble enzyme is a laccase type showing more affinity to various diphenols and paraphenols. Membrane-bound enzyme exists as isoenzymes, showing 3 fractions, of which the slow-moving fraction is capable of oxidizing both 4-methyl catechol and catechol, whereas the two remaining fractions are specific to 4-methyl catechol only. Soluble enzyme exists as a single homogeneous form showing affinity to both mono- and diphenols. Inhibition of the enzyme by potassium iodide and mercuric chloride indicates the active tyrosyl and SH groups of the enzyme. Inhibition of the enzyme by sodium diethyl dithiocarbamate and phenyl thiourea indicates that copper is the prosthetic group of the enzyme.