%0 Journal Article
%T Sources and Applications of Tyrosinase in Life Sciences.
%A Patil M
%A Bhatia M
%A Arvindekar S
%A Patil R
%A Pawar V
%J Curr Pharm Biotechnol
%V 0
%N 0
%D 2024 Jul 15
%M 39021165
%F 2.829
%R 10.2174/0113892010279852240702062859
%X <B>BACKGROUND: </B>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.<BR><B>OBJECTIVE: </B>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.<BR><B>METHODS: </B>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.<BR><B>RESULTS: </B>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.<BR><B>CONCLUSIONS: </B>The article offers a comprehensive exploration of tyrosinase, encompassing its structural features, evolutionary origins, biochemical characteristics, and contemporary applications in various fields.