Abstract
AbstractCytochemical localization of the enzyme phenol oxidase inNeomurraytrema tengrahas 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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