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作 者:龚盛昭[1] 王晓立[1] 林取妹[1] 高晓慧[1]
机构地区:[1]广东轻工职业技术学院轻化工程系,广东广州510300
出 处:《化学研究与应用》2009年第8期1168-1172,共5页Chemical Research and Application
基 金:广东省科技计划项目(2007B080701004)
摘 要: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.The inhibitory effects of methyl cinnamate on the monophenolase activity and diphenolase activity of tyrosinase were studied by enzymological kinetic method in Na2HPO: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 ( 1C50 ) 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 K1 for inhibitor binding with enzyme (E)was 0.66 mmol/L.
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