5α-Reductase inhibitory compounds produced by polymerization of resveratrol with horseradish peroxidase

Abstract

To produce 5α-reductase inhibitory compounds, resveratrol was enzymatically oxidized in a horseradish peroxidase (HRP)/H2O 2 system. Ethyl acetate extract of the oxidation products showed strong 5α-reductase inhibitory activity with 10%-15% organic solvents in the system, whereas without organic solvent little inhibitory activity was exhibited. The optimum pH of enzymatic oxidation for acquisition of the inhibitory activity was 4.5. The inhibitory compounds were isolated and identified as resveratrol trans-dehydrodimer and resveratrol cis-dehydrodimer by comparing with published nuclear magnetic resonance data. The two resveratrol dehydrodimers have stronger inhibitory activity than natural resveratrol dimers and trimers found in Shorea species.