Enzymes phenolase/polyphenol oxidase

Tyrosinase is an enzyme complex (phenolase, polyphenol oxidase are other names which have been used for this enzyme), which catalyses of the ortho hydroxylation of monohydric phenols. The enzyme, which should not be confused with L-tyrosine hydroxylase mentioned above, contains Cu (I) and catalyses two distinct reactions—the hydroxylation of monohydric phenols to o-diphenols (cresolase activity) and the oxidation of o-diphenols to o-quinones (catecholase or catechol oxidase activity) . Most enzymes of this type, which are widely distributed in both the plant and animal kingdoms, exhibit both cataljrtic functions. Thus typically, the conversion of L-tyrosine (5) to L-dopa (15) and dopaquinone (36) which occurs in melanin biosynthesis is catalysed by an enzyme of the tyrosinase category. The two activities appear, in the majority of cases, to be functions of the same enzyme. However, certain o-diphenol oxidases such as those from tea , sweet potato and tobacco have been reported to show no capacity to catalyse the hydroxylation reaction but this is most probably due to destruction of the cresolase activity during purification. 

The products of oxidation are easily visualized shortly after ozone treatments but no claim should be made that phenolics or the oxidative enzymes, polyphenol oxidase, phenolase or peroxidase... 

Phenols are present in chloroplasts (23, 24) and in vacuoles (25) of plant cells. The enzyme polyphenol oxidase and other enzymes of the phenolase complex are bound to the chloroplast lamellae or stroma 27) and in the cytoplasm (26). Although... 

The phenol oxidases probably play no important role in the elimination of phenolic pressor amines, in spite of the importance that has been attached to the oxidation of the catechol nucleus in the past. The names phenolase and cresolase, polyphenol oxidase, and catechol oxidase serve to identify the enzyme with its mono- or diphenolic substrate, but they usually occur together and are difficultly separated. The enzymes have been purified and their characteristics have been described (56, 104, 106, 156). Beyer (21), Alles (5), and Randall and Hitchings (129) have described the relationship of structure of the phenolic pressor amines to the rate of oxidation of their nucleus in the presence of these enzymes. 

Enzymes known as polyphenol oxidases cause enzymatic browning. Other names of the enzyme include phenolases and tyrosinases. The enzymes catalyze the conversion of monophenols and diphenols to quinones. The quinones can undergo a series of non-enzymatic reactions to produce brown, gray and black colored pigments, collectively known as melanins (11). Maillard reactions, caramelizations and ascorbic acid oxidations can produce similar types of colored compounds (12). For some food processing... 

Polyphenol oxidases (e.g., tyrosinase, polyphenolase, phenolase, catechol oxidase, cresolase, catecholase) Chitinolytic enzymes... 

Polyphenol oxidases and ascorbic acid oxidase, which occur in food, are known to have a Cu /Cu redox system as a prosthetic group. Polyphenol oxidases play an important role in the quality of food of plant origin because they cause the enzymatic browning for example in potatoes, apples and mushrooms. Tyrosinases, catecholases, phenolases or cresolases are enzymes that react with oxygen and a large range of mono and diphenols. 

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