Tyrosinase is a multifunctional, glycosylated, and copper-containing oxidase, which catalyzes the first two steps in mammalian melanogenesis and is responsible for enzymatic browning reactions in damaged fruits during post-harvest handling and processing. Neither hyperpigmentation in human skin nor enzymatic browning in fruits are desirable. These phenomena have encouraged researchers to seek new potent tyrosinase inhibitors for use in foods and cosmetics. This article surveys tyrosinase inhibitors newly discovered from natural and synthetic sources. The inhibitory strength is compared with that of a standard inhibitor, kojic acid, and their inhibitory mechanisms are discussed.

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An Updated Review of Tyrosinase Inhibitors

Polyphenol oxidase, a copper-containing metalloprotein, catalyzes the oxidation of phenolic compounds to quinones, which produce brown pigments in wounded tissues. This enzymatic mechanism causes post harvest losses and mainly affects tropical fruits. In this article, some characteristics of polyphenol oxidase from different plants are reviewed and information about conventional and alternative methods to inactivate this enzyme is presented. Characterization of the polyphenol oxidase could help to develop or to choose more effective methods for controlling browning of vegetables and products.

Polyphenol Oxidase: Characteristics and Mechanisms of Browning Control

Inhibitory effect of morin on tyrosinase: Insights from spectroscopic and molecular docking studies

Huang Huang

Papers

Inhibitory effects on mushroom tyrosinase by p-alkoxybenzoic acids

Inhibitory effects of cupferron on the monophenolase and diphenolase activity of mushroom tyrosinase

Unfolding and inactivation of Ampullarium crossean β-glucosidase during denaturation by guanidine hydrochloride