Background: Tyrosinase, often recognized as polyphenol oxidase, plays a pivotal role as an enzyme in catalyzing the formation of melanin-a complex process involving the oxidation of monophenols and o-diphenols.
Objective: Tyrosinase functions as a monooxygenase, facilitating the o-hydroxylation of monophenols to generate the corresponding catechols, as well as catalyzing the oxidation of monophenols to form the corresponding o-quinones, exhibiting diphenolase or catecholase activity. This versatile enzymatic capability is not limited to specific organisms but is found across various sources, including bacteria, fungi, plants, and mammals.
Method: Pertinent research articles, reviews, and patents on tyrosinase were gathered through a comprehensive literature search. These materials were analyzed to gain insights into the diverse applications of tyrosinase. The review was structured by categorizing these applications and offering a thorough summary of the current state of knowledge in the field.
Result: Based on the literature survey, tyrosinase exhibits promising potential across a spectrum of biotechnological applications. These include but are not limited to: synthesizing L-DOPA, creating innovative mixed melanins, manufacturing phenolic biosensors, deploying in food and feed industries, facilitating protein cross-linking, eliminating phenols and dyes, and serving as a biocatalyst. Moreover, immobilized tyrosinase demonstrates multiple utility avenues within the pharmaceutical sector.
Conclusion: The article offers a comprehensive exploration of tyrosinase, encompassing its structural features, evolutionary origins, biochemical characteristics, and contemporary applications in various fields.
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