Biotransformation of mulberroside A from Morus alba results in enhancement of tyrosinase inhibition
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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.
KeywordsBiotransformation Mulberroside A Oxyresveratrol Tyrosinase inhibitor
This study was supported by the Technology Development Program for Agriculture and Forestry, Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea.
- 8.Habauzit V, Nielsen IL, Gil-Izquierdo A, Trzeciakiewicz A, Morand C, Chee W, Barron D, Lebecque P, Davicco MJ, Williamson G, Offord E, Coxam V, Horcajada MN (2009) Increased bioavailability of hesperetin-7-glucoside compared with hesperidin results in more efficient prevention of bone loss in adult ovariectomised rats. Br J Nutr 102:976–984CrossRefPubMedGoogle Scholar
- 21.Nielsen IL, Chee WS, Poulsen L, Offord-Cavin E, Rasmussen SE, Frederiksen H, Enslen M, Barron D, Horcajada MN, Williamson G (2006) Bioavailability is improved by enzymatic modification of the citrus flavonoid hesperidin in humans: a randomized, double-blind, crossover trial. J Nutr 136:404–408PubMedGoogle Scholar
- 25.Rooseboom M, Commandeur JN, Vermeulen NP (2004) Enzyme-catalyzed activation of anticancer prodrugs. Parmacol Rev 56:53–102Google Scholar