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.
| Original language | English |
|---|---|
| Pages (from-to) | 631-637 |
| Number of pages | 7 |
| Journal | Journal of Industrial Microbiology and Biotechnology |
| Volume | 37 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2010 Jun |
Bibliographical note
Funding Information:This study was supported by the Technology Development Program for Agriculture and Forestry, Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea.
Keywords
- Biotransformation
- Mulberroside A
- Oxyresveratrol
- Tyrosinase inhibitor
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology