Natural and Synthetic Tyrosinase Inhibitors as Antibrowning Agents: An Update

Abstract

Tyrosinase (EC 1.14.18.1), a copper-containing enzyme, can cause enzymatic browning in raw fruits, vegetables, and beverages. Browning is an undesirable reaction that is responsible for less attractive appearance and loss in nutritional quality. These phenomena have encouraged researchers to seek new potent tyrosinase inhibitors for use in the food industry. This article reviews recent studies on tyrosinase inhibitors of natural and synthetic origins. The information offered here should help food industry in developing and using potential tyrosinase inhibitors desirable efficacy and safety, and for improving food quality.

Blaj white wines characterization

“…Tyrosinase is an important enzyme involved in melanin biosynthesis [22]. Extracts and compounds which show anti-tyrosinasic inhibitory activity are useful whitening agents in cosmetics or additives in food industry to prevent fruits enzymatic browning phenomenon [23].…”

A Study of the Whitening Activities of Magnolia obovata Bark Ethyl Acetate Fractions as Cosmetic Ingredient

“…멜라닌 생성에 관여하는 주요 효소인 tyrosinase와 tyrosinase-related protein 1 (TRP-1), tyrosinase-related protein 2 (TRP-2)의 발현에 관여하는 전사인자 MITF는 이들 유전자를 과발현 시켜 멜라닌 을 합성시킨다 [9][10][11]. 자외선이나 염증 등의 외부 자극 에 의해서도 멜라닌 생성이 촉진되므로 이러한 자극을 줄이거나, 자극이 melanocyte로 전달되는 신호를 차단 하거나 [12][13][14][15], 멜라닌 색소 생성 효소인 tyrosinase의 합성을 저해하는 방법 등이 있을 수 있다 [16,17].…”

Tyrosinase Inhibition, 2,2-Diphenyl-1-Picrylhydrazyl Radical Scavenging Activity, and Phytochemical Screening of Fractions and Ethanol Extract From Leaves and Stem Bark of Matoa (Pometia Pinnata)

“…The compound content caused the matoa leaves and stem bark extracts to have very strong DPPH scavenging activity, but both extracts did not have good tyrosinase inhibitory ability. This might be because the polyphenolic compounds in both extracts were mostly in the form of glycosides, which gave the polyphenolic compounds less ability to bind and inhibit the action of tyrosinase enzyme [20].…”

“…The tyrosinase inhibitory ability of the phenolic compounds was strongly influenced by the structure of the phenolic compounds. The amount and position of the hydroxyl groups of the B ring and the substitution of the hydroxyl groups as well as their steric constraints played an important role in the inhibition of phenolic compounds against tyrosinase activity [20]. For example, quercetin and kaempferol were known to be flavonoid compounds with activity as tyrosinase inhibitors [6].…”