作　　者： ; ; ; ; ;

机构地区： 华南理工大学轻工与食品学院

出　　处： 《食品工业科技》 2012年第11期53-55,共3页

摘　　要： 研究二氢杨梅素与胰蛋白酶相互作用特性,测定二氢杨梅素与胰蛋白酶反应前后胰蛋白酶催化活力、荧光光谱的变化和二氢杨梅素清除ABTS+.能力的变化。二氢杨梅素与胰蛋白酶在37℃下反应10min后,酶催化活力及二氢杨梅素清除ABTS+.能力都有明显减弱。同时,二氢杨梅素可使胰蛋白酶发生荧光猝灭,猝灭类型为静态猝灭,猝灭常数Kq是2.3180×1012(mol/L)-1S-1,结合位点数n为0.6819。 The interaction between dihydromyricetin（DMY） and trypsin was studied by measuring the catalytic activity,the change in the antioxidant activity and fluorescence spectra after being interacted with trypsin, After treatment for 10min at 37~C,dihydromyricetin led to the inhibition of catalytic activity. Trypsin could mask the total antioxidant capacity by scavenging ABTS DMY led the quenching of intrinsic fluorescence of trypsin in physiological condition. With fluorescence quenching method,the quenching constant Kq was found to be 2.3180×10^12（mol/L）-1S-1 and the number of binding site N was 0.6819.

关 键 词： 二氢杨梅素 胰蛋白酶 酶活性 荧光 抗氧化

领　　域： [轻工技术与工程] [轻工技术与工程]