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对羟基肉桂酸乙酯对胰脂肪酶的抑制作用及机理 被引量:8

Inhibitory Effect and Mechanism of Ethyl p-hydroxycinnamate on Pancreatic Lipase
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摘要 为探究对羟基肉桂酸乙酯的降脂活性,本文采用酶反应动力学和分子对接技术来研究对羟基肉桂酸乙酯对胰脂肪酶的抑制类型和抑制机理。抑制动力学结果表明,对羟基肉桂酸乙酯对胰脂肪酶表现为可逆竞争型抑制(半抑制浓度IC50为41.07μg/mL),其最大反应速率Vmax为2.61μmol/L·min,抑制常数Ki为114.35μg/mL;分子对接结果表明,对羟基肉桂酸乙酯可以与胰脂肪酶催化三联体中的氨基酸残基Ser152和His263形成强烈的氢键作用,且通过范德华力、氢键作用力和疏水作用力与胰脂肪酶的氨基酸残基作用,与底物p-NPB竞争酶的活性中心位点。本研究为对羟基肉桂酸乙酯在降脂功能食品中的应用提供了一定的理论依据。 In order to explore lipid lowering activity of ethyl p-hydroxycinnamate,enzyme reaction kinetics and molecular docking techniques were used to study the inhibitory type and mechanism of ethyl p-hydroxycinnamate on pancreatic lipase.The kinetics results showed that ethyl p-hydroxycinnamate was a reversible competitive inhibitor of pancreatic lipase(semi-inhibitory concentration IC50 was 41.07μg/mL),with the maximum reaction rate Vmax of 2.61μmol/L·min and the inhibitory constant Ki of 114.35μg/mL.Molecular docking results showed that ethyl p-hydroxycinnamate could form a strong hydrogen bond with the amino acid residues Ser152 and His263 in the triplet catalyzed by pancreatic lipase.Ethyl phydroxycinnamate could interacted with the amino acid residues of pancreatic lipase through Van der Waals force,hydrogen bond force,and competed with the substrate p-NPB for the active site of the enzyme.This study provided a theoretical basis for the application of ethyl p-hydroxycinnamate in functional foods.
作者 于洋君 伍菱 何君竹 倪辉 杨远帆 YU Yangjun;WU Ling;HE Junzhu;NI Hui;YANG Yuanfan(Jimei University,College of Food and Biological Engineering,Xiamen 361021,China;Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering,Xiamen 361021,China;Research Center of Food Biotechnology of Xiamen City,Xiamen 361021,China)
出处 《食品工业科技》 CAS 北大核心 2021年第9期94-99,共6页 Science and Technology of Food Industry
关键词 对羟基肉桂酸乙酯 胰脂肪酶 抑制作用 分子对接 ethyl p-hydroxycinnamate pancreatic lipase inhibitory effect molecular docking
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