The inhibitory effects of methyl cinnamate on the monophenolase activity and diphenolase activity of tyrosinase were studied by enzymological kinetic method in Na2HPO4-NaH2PO4 buffer solution(pH=6.8) at 30 ℃.Methyl cinnamate was found to inhibit the monophenolase activity and diphenolase activity of tyrosinase.The methyl cinnamate concentration leading to 50 % inhibitory rate(IC50) were 0.61 mmol/L for monophenolase activity and 1.49 mmol/L for diphenolase activity,respectively.Methyl cinnamate coued extend the lag time of monophenolase.0.8 mmol/L of methyl cinnamate resulted in the lag time extension from 1.1 min to 3.2 min.The inhibition kinetics analyzed by Lineweaver-Burk plots indicated that methyl cinnamate was a noncompetitive inhibitor to diphenolase,and the inhibition constant KI for inhibitor binding with enzyme(E)was 0.66 mmol/L.
