Title
Tyrosinase inhibitory mechanism of betulinic acid from Dillenia indica
Author
Rajarshi Biswas, Joydeb Chanda, Amit Kar, Pulok K. Mukherjee
Year
2017
Journal
Food Chemistry
Abstract
The fruit of Dillenia indica L. is extensively used as a food additive. Betulinic acid (BA) is the most prominent secondary metabolite present in D. indica. This study screened the bioassay guided isolation of BA from D. indica and explored its tyrosinase inhibitory mechanism. Half maximal inhibitory concentration (IC50) of BA were calculated as 13.93 µM and 25.66 µM for diphenolase and monophenolase. Enzyme kinetic analysis revealed that BA inhibited tyrosinase activity non-competitively. Further, conformational analysis of tyrosinase with BA was measured by fluorescence and circular dichroism spectroscopy. These results implied that diminish rigidity of enzyme might disturb the catalytic conformation of tyrosinase. Moreover, In-silico analysis confirmed probable binding polar and non-polar region on the active site of tyrosinase. Based on these findings, we suggest that BA from D. indica may be useful in preventing enzymatic browning reactions in food products.
Instrument
J-815
Keywords
Circular dichroism, Secondary structure, Ligand binding, Biochemistry, Food science