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J Ind Microbiol Biotechnol. 2010 Jun;37(6):631-7. doi: 10.1007/s10295-010-0722-9. Epub 2010 Apr 22.

Biotransformation of mulberroside A from Morus alba results in enhancement of tyrosinase inhibition.

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  • 1Department of Chemical Engineering and Biotechnology, Korea Polytechnic University, Shihung-si, Kyunggi-do 429-793, South Korea.

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.

PMID:
20411402
[PubMed - indexed for MEDLINE]
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