Affiliation:
1. Department of Pharmaceutical Chemistry, Bharati Vidyapeeth College of Pharmacy, Kolhapur, Maharashtra, 416013,
India
Abstract
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.
Publisher
Bentham Science Publishers Ltd.