Title |
Biotransformation of mulberroside A from Morus alba results in enhancement of tyrosinase inhibition
|
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Published in |
Journal of Industrial Microbiology & Biotechnology, April 2010
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DOI | 10.1007/s10295-010-0722-9 |
Pubmed ID | |
Authors |
Jeong-Keun Kim, Mijin Kim, Ssang-Goo Cho, Myung-Kyoo Kim, Suhng Wook 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 IC(50) of 53.6 and 0.49 microM, 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. |
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