柚皮素对α-葡萄糖苷酶的抑制作用及其机制  

Inhibitory Effect of Naringin onα-Glucosidase and Its Mechanism

作　　者：周香菊 陈雨琴 尹忠平[1] 梁琦 臧建威 唐道邦[2] 陈继光[1] ZHOU Xiangju;CHEN Yuqin;YIN Zhongping;LIANG Qi;ZANG Jianwei;TANG Daobang;CHEN Jiguang(College of Food Science and Engineering,Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control,Jiangxi Agricultural University,Nanchang 330045,China;Institute of Sericulture and Agro-Products Processing,Guangdong Academy of Agricultural Sciences,Guangdong Key Laboratory of Agro-Products Processing/Key Laboratory of Functional Food,Guangzhou 510610,China)

机构地区：[1]江西农业大学食品科学与工程学院,江西省天然产物与功能食品重点实验室/江西省农产品加工与安全控制工程实验室,江西南昌330045 [2]广东省农业科学院蚕业与农产品加工研究所,广东省农产品加工重点实验室/功能食品重点实验室,广东广州510610

出　　处：《食品工业科技》2022年第8期157-164,共8页Science and Technology of Food Industry

基　　金：国家自然科学基金项目(31460436);国家自然科学基金项目(31960515);广州市科技计划项目(201909020001);江西省自然科学基金项目(20192BAB204004)。

摘　　要：为研究柚皮素对α-葡萄糖苷酶的抑制作用,本文采用酶动力学、荧光光谱和分子对接等方法研究了柚皮素对α-葡萄糖苷酶的抑制效果、抑制作用类型及其抑制作用的分子机制。柚皮素对α-葡萄糖苷酶的IC_(50)为0.174 mmol/L,显著低于阿卡波糖的0.721 mmol/L,为非竞争型抑制剂,K_(i)值为0.114 mmol/L;柚皮素和α-葡萄糖苷酶的结合导致了酶分子的内在荧光静态猝灭,猝灭常数为0.1598×10^(4)L/mol,结合位点数n为1。分子对接结果显示,在氢键、离子键、疏水作用、π-πT型堆积、静电作用五种作用力的驱动下,柚皮素结合于α-葡萄糖苷酶分子的一个疏水口袋中,结合能为-7.6 kJ/mol。本文研究结果表明,柚皮素是一种较好的食源性α-葡萄糖苷酶抑制剂,在辅助治疗糖尿病功能食品中具有良好的应用前景。To investigate the inhibitory activity and mechanism of naringin on α-glucosidase,the inhibition effect,type,and molecular mechanism of naringin on α-glucosidase were investigated by integrative analysis of enzyme kinetics,fluorescence spectroscopy and molecular docking simulation.The results showed that IC_(50) of naringin againstα-glucosidase was 0.174 mmol/L,which was significantly lower than that of acarbose(IC_(50)=0.721 mmol/L).The inhibition type was non-competitive inhibition with a K_(i) of 0.114 mmol/L.The binding of naringin andα-glucosidase led to the internal fluorescence quenching of the enzyme molecule.Furhter analysis indicated that the quenching constant was 0.1598×10^(4)L/mol,and there was only one binding site.The molecular docking results showed that naringin was bound to a hydrophobic pocket ofα-glucoside enzyme by the driving force of hydrogen bond,ionic bond,hydrophobic action,π-π-T stacking,and electrostatic action,with a binding energy of-7.6 kJ/mol.The results indicated that naringin was a good foodborneα-glucosidase inhibitor,and therefore had a good application prospect in the adjuvant treatment of diabetes functional food.

关 键 词：柚皮素 Α-葡萄糖苷酶 荧光光谱 分子对接 抑制 

分 类 号：R284.1[医药卫生—中药学]