An Updated Review of Tyrosinase Inhibitors

By Te-Sheng Chang. International Journal of Molecular Sciences, 2009

1,500 citations recorded by the source corpus.

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.

Subfields: Biochemistry, Cell Biology, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/550a6d90e31c31b86b87482965325d33d2a32e06

Citations in the corpus

• Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone. (2011, neutral): “57,58 The Ab TYR crystal structure may take this search from the ad-hoc nature that it has had until now to a more directed and targeted e ff ort for this commercially important enzyme.”