Tyrosinase (Polyphenol Oxidase)

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[ Source ] Mushroom
[ Appearance ] Light yellow to dark brown powder or liquid

About Tyrosinase (Polyphenol Oxidase)
Polyphenol oxidase is an oxygen transferase. In addition to the use of oxygen to catalyze the dehydrogenation of catechol to generate o-quinones, and the o-hydroxylation of phenols to catechols, it also has oxidase activity.
Polyphenol oxidases are terminal oxidases that transfer electrons directly to molecular oxygen. Its main function in tea is to catalyze the formation of catechins into ointments, and further form theaflavins and other pigments and aroma components.
Polyphenol oxidase is a bifunctional, copper ion-containing oxidase with both catecholase and cresolase activities involved in browning reactions. Polyphenol oxidase is a tetramer containing 4 copper atoms and 2 binding sites for aromatic compounds per molecule, including phenolic substrates. Also contains a distinct oxygen-copper binding site. Copper may be in the cuprous state (Cu+) and inactivation of the enzyme involves oxidation of Cu+ to Cu2+.