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 c...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.展开更多
文摘采用酶动力学方法研究了香草酸对酪氨酸酶单酚酶和二酚酶活力的抑制效应。结果表明,香草酸对酪氨酸酶单酚酶和二酚酶活性均有抑制作用,导致单酚酶活力和二酚酶活力下降50%的香草酸浓度(IC50)约分别为1.3 mmol/L和2.6 mmol/L。香草酸能明显延长单酚酶的迟滞时间,2 mmol/L香草酸能使迟滞时间由1.1 m in延长至4.7 m in。香草酸对二酚酶的抑制作用表现为混合型抑制,对游离酶的抑制常数(KI)和对酶-底物络合物的抑制常数(KIS)分别为1.76 mmol/L和8.57 mmol/L。
文摘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.
