摘要
通过测定槲皮素对胰蛋白酶催化活性、催化反应动力学以及内源荧光光谱的影响,对槲皮素和胰蛋白酶相互作用特性进行研究。结果表明:槲皮素对胰蛋白酶催化活性有明显的抑制作用,当槲皮素与胰蛋白酶的摩尔比为44:1,在37℃反应10min,抑制率达到32.5%;反应时间对两者的作用影响并不明显;槲皮素对胰蛋白酶催化活性的抑制作用属于可逆的竞争性抑制;槲皮素可使胰蛋白酶的内源荧光发生猝灭现象,猝灭常数Kq是4.7415×1012(mol/L)-1.S-1,猝灭类型为静态猝灭,结合位点数N为0.9206。
The interaction between quereetin and trypsin was studied by measuring the catalytic activity, the enzymatic kinetic analysis and fluorescence spectra. Quercetin showed inhibition effect on catalytic activity of trypsin. When trypsin was treated by quercetin with the molar ratio of quercetin to trypsin of 44：1 for 10rains under 37 ℃, the inhibition rate reached 32.5%. Reaction time had little effect on the inhibition rate. The type of inhibition effect was reversible competitive inhibition. Quercetin can cause the quenching of intrinsic fluorescence of trypsin in physiological condition. With fluorescence quenching method, the quenching constant Kq was found to be 4.7415×10^12（mol/L）-1.S-1 and the number of binding site N was 0.9206.
出处
《现代食品科技》
EI
CAS
北大核心
2012年第3期260-262,266,共4页
Modern Food Science and Technology
基金
国家自然科学基金项目(21002034)
关键词
胰蛋白酶
槲皮素
酶活力
酶动力学
荧光光谱
trypsin
quercetin
enzymatic activity
fluorescence spectra
enzyme kinetics
