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- Title
Biotransformation of mulberroside A from Morus alba results in enhancement of tyrosinase inhibition.
- Authors
Jeong-Keun Kim; Mijin Kim; Ssang-Goo Cho; Myung-Kyoo Kim; Suhng Kim; Young-Hee Lim
- Abstract
Mulberroside A, a glycosylated stilbene, was isolated and identified from the ethanol extract of the roots of Morus alba. Oxyresveratrol, the aglycone of mulberroside A, was produced by enzymatic hydrolysis of mulberroside A using the commercial enzyme Pectinex®. Mulberroside A and oxyresveratrol showed inhibitory activity against mushroom tyrosinase with an IC50 of 53.6 and 0.49 μM, respectively. The tyrosinase inhibitory activity of oxyresveratrol was thus approximately 110-fold higher than that of mulberroside A. Inhibition kinetics showed mulberroside A to be a competitive inhibitor of mushroom tyrosinase with l-tyrosine and l-DOPA as substrate. Oxyresveratrol showed mixed inhibition and noncompetitive inhibition against l-tyrosine and l-DOPA, respectively, as substrate. The results indicate that the tyrosinase inhibitory activity of mulberroside A was greatly enhanced by the bioconversion process.
- Publication
Journal of Industrial Microbiology & Biotechnology, 2010, Vol 37, Issue 6, p631
- ISSN
1367-5435
- Publication type
Academic Journal
- DOI
10.1007/s10295-010-0722-9