栀子黄对淀粉消化酶的抑制动力学及相互作用研究
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河南省自然科学基金项目(182300410079)


Studies on the Inhibition Kinetics and Interaction Mechanism of Gardenia Yellow on Starch Digestive Enzyme
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    摘要:

    α-淀粉酶和α-葡萄糖苷酶是淀粉消化关键酶,也是治疗Ⅱ型糖尿病的关键酶。利用酶抑制动力学和荧光光谱技术研究栀子黄对α-淀粉酶和α-葡萄糖苷酶的抑制活性及其互作机制。结果表明,栀子黄以竞争性方式抑制α-淀粉酶和α-葡萄糖苷酶,其缔合常数Kic分别为1.47 mg/mL和0.58 mg/mL。荧光光谱表明:栀子黄对α-淀粉酶和α-葡萄糖苷酶的内源荧光有较强的猝灭能力,通过Stern-Volmer方程得到栀子黄对α-淀粉酶和α-葡萄糖苷酶的猝灭是以静态猝灭为主的混合型猝灭。焓和熵的变化表明:栀子黄与葡萄糖苷酶的结合主要由范德华力和疏水相互作用驱动,结合距离分别为4.77 nm和5.19 nm。同步荧光表明,栀子黄与α-淀粉酶和α-葡萄糖苷酶的结合引起酶的重排和构象变化,从而引起酪氨酸残基或/和色氨酸残基的变化。

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    α-amylase and α-glucosidase are key enzymes in starch digestion and treatment of type Ⅱ glycosuria. The inhibitory activity and interaction mechanism of gardenia yellow(GY) on α-amylase and α-glucosidase were studied by enzyme inhibition kinetics and fluorescence spectroscopy. The results showed that gardenia yellow inhibited α-amylase and α-glucosidase in a competitive manner, and its association constant Kic was 1.47 mg/mL and 0.58 mg/mL, respectively. The fluorescence spectra showed that gardenia yellow had strong quenching ability to the endogenous fluorescence of α-amylase and α-glucosidase, and the mixed quenching of gardenia yellow on α-amylase and α-glucosidase was mainly static quenching through Stern-volmer equation. The changes of enthalpy and entropy showed that the binding of gardenia yellow to glucosidase was mainly driven by Van Der Waals force and hydrophobic interaction, and the binding distance was 4.77 nm and 5.19 nm. Synchronous fluorescence showed that the binding of gardenia yellow with α-amylase and α-glucosidase caused enzyme rearrangement and conformational change, resulting in the change of tyrosine residue or/and tryptophan residue.

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任顺成;万毅;李林政;潘天义.栀子黄对淀粉消化酶的抑制动力学及相互作用研究[J].中国食品学报,2021,21(9):38-47

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  • 在线发布日期: 2021-10-19
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