Phytochemical Screening, Tyrosinase Inhibitory Effects and Kinetics of Cam Wood Dye Extracts
Advances in Biochemistry
Tyrosinase is a key enzyme in melanin biosynthesis, as it catalyzes the oxidation of o-diphenols to o-quinones. Cam wood dye was extracted using methanol, acetone and dichloromethane; while extracts obtained were screened for Phytochemicals as well as their tyrosinase inhibitory effects and kinetic studies. Phytochemical screening of the three extracts showed the presence of total phlobatanins in all extracts except methanolic which had minute presence. Cardiac glycosides and flavonoids were
... o observed in the dichloromethane extracts and methanolic extract respectively. The methanolic extracts had best enzyme inhibition (84.1%) at highest concentration considered of 400µg/ml as compared to the dichloromethane and acetone extracts with peak values of 58.5 and 51.5% respectively. The enzyme kinetics analysis of substrate showed same inhibition type for three extracts which was non-competitive and its mechanism irreversible. The Michealis-Mentens constants for the three extracts were determined to be 0.344, 0.355 and 0.214mM, for acetone, dichloromethane and methanolic extracts respectively while the values of V max /K m shows inhibiting extracts followed the order: methanol extract > acetone extract > dichloromethame extract. The result therefore showed that methanolic extracts of Cam wood dye was the most effective in tyrosinase inhibition.