An examination of natural and synthetic tyrosinase inhibitors

Abstract

The enzyme responsible for this process is known as tyrosinase, which is sometimes referred to as polyphenol oxidase, monophenol oxidase, phenolase, or catecholase. It is present in humans, plants, microbes, and fungi. Melanin pigments, found in both plants and animals, require this enzyme as an essential component. Tyrosinase is present in animal creatures, particularly in the pigments of the skin, hair, and eyes. Tyrosinase can cause darkening in foods that is unrelated to their inherent color. Beverages such as fruit juice and wine may experience a decline in appearance and flavor, as well as the occurrence of turbidity and precipitation. The unwanted phenomenon of browning in fruits and vegetables, which is frequently caused by enzymatic processes, needs to be avoided. Tyrosinase enzyme inhibitors are employed to hinder the catalytic oxidations that lead to browning by the tyrosinase enzyme. Currently, these basic ingredients are commonly found in skin whitening solutions, particularly in the field of cosmetics. In addition, tyrosinase inhibitors have practical applications in the treatment of skin problems associated with melanin pigmentation. Furthermore, tyrosinase inhibitors competitively and reversibly hinder the activity of human melanocyte tyrosinase, hence impeding the production of melanin.Numerous substances possess the ability to hinder the activity of the enzyme tyrosinase. Ongoing studies are being conducted on several derivatized compounds to increase inhibition. This article explores the inhibitory effects of many compounds, including kojic acid, azelaic acid, flavonoids, arbutin-deoxyarbutin, curcumin and its derivatives, and copper chelators, on the enzyme tyrosinase.