What is tyrosinase inhibition activity?
Furthermore, tyrosinase is a key rate-limiting enzyme that can catalyze enzyme browning and melanin synthesis. Tyrosinase inhibitors capable of inhibiting the biosynthesis of melanin are used currently in various hyperpigmentation and cosmetic agents to control the formation of freckles [7, 8].
Why is inhibition of tyrosinase important?
Melanin plays an important role in protecting human skin from the harmful effects of UV radiation from the sun. Melanin also determines our phenotypic appearance. These phenomena have encouraged researchers to seek new potent tyrosinase inhibitors for use in antibrowning of foods and skin whitening.
What inhibits melanin by inhibiting tyrosinase?
Arbutin, a prodrug of hydroquinone, is a natural product and reduces or inhibits melanin synthesis by inhibiting tyrosinase.
What is the best tyrosinase inhibitor?
Tyrosinase Inhibitors
- Hydroquinone – Very powerful Tyrosinase Inhibitors.
- Kojic Acid – a natural crystal like substance that is used is some skin whitening products.
- Arbutin – a glycosylated form of Hydroquinone but more gentle, found in Bearberry, Paper Mulberry, Blueberry and Cranberry.
How does vitamin C inhibit tyrosinase?
Vitamin C can indirectly inhibit the activity of tyrosinase because of its antioxidant capacity, thus reducing melanogenesis. Furthermore, vitamin C can also reduce the melanogenesis of melanoma cells stimulated by α-melanocyte-stimulating hormone (α-MSH) in vitro (Stojkovic-Filipovic and Kittler, 2014).
Why is tyrosinase important?
Tyrosinase is responsible for the first step in melanin production. It converts a protein building block (amino acid) called tyrosine to another compound called dopaquinone.
How do you reduce tyrosinase activity?
Chang (2009) discussed several ways to achieve anti-tyrosinase activity. It can be done by the reducing agents such as ascorbic acid, which can reduce o-dopaquinone to dopa or by the o-dopaquinone scavenger such as thio-containing compounds, which can react with dopaquinone to form colorless products.
Does ferulic acid inhibit tyrosinase?
Ferulic acid reduced tyrosinase activity by directly binding to the enzyme, whereas no binding was observed between caffeic acid and tyrosinase. Our analysis revealed that both substances also inhibited the CK2-mediated phosphorylation of tyrosinase.