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Studies on the enzyme phenol oxidase in a freshwater monogenetic trematode
Published online by Cambridge University Press: 05 June 2009
Abstract
Cytochemical localization of the enzyme phenol oxidase in Neomurraytrema tengra has been studied. Results reveal that the enzyme reacts with substrates such as catechol, hydroquinone, pyrogallol, dopa, doparmine, epinephrine and tyramine, but not with tyrosine and protocatechuic acid. Thus it shows activity with a wide range of phenols, aminated, mono and diphenols and also with deaminated and decarboxylated, di- and polyphenols. The maximum activity of the enzyme occurs between 40°C and 50°C with a pH optimum of 6–6.
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