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Pectin enhances the inhibition of α-amylase via the mixture of rutin and quercetin

文献类型： 外文期刊

作者： Qin, Yajuan 1 ; Chen, Xiaoai 2 ; Xu, Fei 2 ; Zhu, Kexue 2 ; Wang, Ping 3 ; Zhang, Yutong 2 ; Zhang, Yanjun 2 ;

作者机构： 1.Chinese Acad Agr Sci, Natl Nanfan Res Inst Sanya, Sanya 572024, Peoples R China

2.Chinese Acad Trop Agr Sci, Spice & Beverage Res Inst, Wanning 571533, Hainan, Peoples R China

3.Northeast Forestry Univ, Sch Forest, Harbin 150040, Heilongjiang, Peoples R China

4.Natl Ctr Important Trop Crops Engn & Technol Res, Wanning 571533, Hainan, Peoples R China

5.Key Lab Proc Suitabil & Qual Control Special Trop, Wanning 571533, Hainan, Peoples R China

6.Chinese Acad Trop Agr Sci, Sanya Res Inst, Sanya 572025, Peoples R China

关键词： Rutin-quercetin mixture; Pectin; alpha-Amylase

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2025 年 285 卷

页码：

收录情况： SCI

摘要： The human dietary system, which contains a variety of compounds such as polyphenols and polysaccharides, is very complex. Whether polysaccharides affect the inhibitory of polyphenol mixtures on alpha-amylase needs to be further investigated. The aim of this study was to analyze the effect and mechanism of pectin on the inhibition of alpha-amylase by a mixture of rutin and quercetin (R-Q). Results revealed that the inhibition and quenching affinity of R-Q for alpha-amylase was enhanced by pectin. The Stern-Volmer quenching constant of R-Q-alpha-amylase was increased by pectin from (6.08 +/- 0.453) x 103 mL/mg to (9.80 +/- 0.285) x 103 mL/mg. Pectin enhanced the ability of R-Q to inhibit alpha-amylase for two main reasons. On the one hand, it was owing to the binding of pectin to rutin, which increased the opportunity for quercetin to bind to the active center of alpha-amylase, thus enhancing the inhibitory effect of R-Q on alpha-amylase. On the other hand, pectin and quercetin simultaneously bound to different sites of alpha-amylase by noncovalent interactions to form the ternary complex of pectin-alpha-amylase-quercetin. The conformation of alpha-amylase and the hydrophobicity of amino acid residues were altered by the ternary complex, thereby enhancing the hydrogen bonding in the reaction system.

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