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2025, 08, v.36 24-30
基于分子对接探究三七皂苷对α-淀粉酶活性的抑制作用
基金项目(Foundation):
邮箱(Email): 1459519459@qq.com;
DOI: 10.19804/j.issn1006-2513.2025.8.004
摘要:

本研究探讨了三七皂苷对α-淀粉酶活性的抑制作用,研究了其抑制率、抑制类型、抑制动力学及分子对接特征,并探究了pH值和温度对三七皂苷酶活抑制能力的影响。结果发现:三七皂苷能够降低α-淀粉酶活性,且抑制效果随三七皂苷浓度的增加而增强;三七皂苷以混合竞争的方式抑制α-淀粉酶活性;三七皂苷能够通过氢键、疏水相互作用以及盐桥与α-淀粉酶结合,其结合能为-7.76 kcal/mol,表明其具有较强的结合亲和力;当pH低于5或高于9时,三七皂苷对α-淀粉酶活性的抑制能力显著下降;在温度超过55℃的条件下处理后,三七皂苷的抑制效果也受到负面影响。以上结果表明,三七皂苷能够同时与底物结合,并干扰酶的活性位点,从而降低其催化效率。此外,三七皂苷在中性环境(pH 5~7)和低温条件(低于35℃)下表现出较好的稳定性,对α-淀粉酶活性具有显著的抑制活性。

Abstract:

The inhibitory effect of Panax notoginseng saponins on activity of α-amylase was investigated by examining its inhibition rate,inhibition type,inhibition kinetic parameters,and molecular docking characteristics. Additionally,the effects of pH and temperature on the inhibition stability of ginsenosides was explored. The results showed that:Ginsenosides could reduce the activity of α-amylase,with the inhibitory effect increasing as the concentration of Panax notoginseng saponins increased. Panax notoginseng saponins inhibited the activity of α-amylase in a mixed competitive manner. Ginsenosides interacted with α-amylase through hydrogen bonds,hydrophobic interactions,and salt bridges,with a binding energy of-7.76 kcal/mol,demonstrating a strong binding affnity. The inhibitory capacity of ginsenosides on α-amylase activity decreased when the pH was below 5 or above 9. Treatment at temperatures exceeding 55 ℃ negatively affected the inhibition effciency. The above results showed that Panax notoginseng saponins could both bind to the substrate and interfere with the active site of enzyme,thereby reducing its catalytic effciency. Furthermore,Panax notoginseng saponins exhibited better stability and signifcant inhibitory activity against α-amylase under neutral environments( pH 5~7) and at low temperatures(below 35 ℃).

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基本信息:

DOI:10.19804/j.issn1006-2513.2025.8.004

中图分类号:TS201.25

引用信息:

[1]汤莹莹,潘江凌,潘劲松,等.基于分子对接探究三七皂苷对α-淀粉酶活性的抑制作用[J].中国食品添加剂,2025,36(08):24-30.DOI:10.19804/j.issn1006-2513.2025.8.004.

基金信息:

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