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》 2013年第22期88-90,95,共4页

摘　　要： 采用酶动力学方法和荧光光谱法研究山奈酚对α-淀粉酶的抑制作用。在pH6.8、37℃条件下反应20min,山奈酚(1mg/mL,0.05mL)对α-淀粉酶(0.328U/mL,0.2mL)催化活性的抑制率达到24.39%。该抑制过程是以非竞争性方式进行。同时,山奈酚对α-淀粉酶的内源荧光产生有规律的猝灭作用,以静态猝灭方式为主。二者自发结合形成复合物,其主要作用力为疏水作用,有1个结合位点。 The inhibitory effect of kaempferol on α-amylase had been studied by enzymatic kinetics and fluorescence spectroscopy. Results indicated that kaempferol showed inhibition effect on the catalytic activity of a-amylase. The type of inhibition effect was a noncompetitive ihibition, α-Amylase （0.328U/mL,0.2mL） was treated by kaempferol（1mg/mL,0.05mL） under pH6.8,37℃ for 20min,the inhibition rate reached 24.39%. The regular quenching of intrinsic fluorescence of α-amylase could be induced by kaempferol as a quencher in physiological condition,and the quenching mechanism was a static quenching. Kaempferol could bind spontaneously with α-amylase to form a new complex by hydrophobic. There was only one binding constant between kaempferol and α-amylase.

关 键 词： 山奈酚 淀粉酶 酶动力学 荧光光谱

领　　域： [轻工技术与工程] [轻工技术与工程]