Glandular hair constituents of Mallotus philippinensis Muell. fruit act as tyrosinase inhibitors: Insights from enzyme kinetics and simulation study

Abstract

The glandular hair extracts from the fruit rind of Mallotus philippinensis Muell. is employed to treat various skin infections, however the anti-tyrosinase activity remains unknown. Hence the present study inspected on the anti-melanogenic activity of M. philippinensis constituents. Lineweaver Burk plot revealed mixed inhibition for Rottlerin; non-competitive type of inhibition for mallotophilippen A and B respectively. Thermodynamic studies resulted in static quenching forming ground state complex with higher binding constant temperature dependently. Fluorescence and circular dichroism study implicated conformational change in secondary and tertiary structure of tyrosinase. Molecular docking suggests rottlerin has high binding affinity to the active site pocket of tyrosinase. Simulation study further proved that the compactness of inhibitor with tyrosinase by hydrogen bonding influenced the stability of the enzyme. Depigmentation efficacy is further proved in Aspergillus niger spores. Thus our findings delineate that rottlerin could be utilized as a depigmentation agent in food pharmaceutical and agricultural industries.

Keywords: Mallotophilippen A; Mallotophilippen B; Mallotus philippinensis; Rottlerin; Tyrosinase.