体外模拟胃部消化对白芸豆α-淀粉酶抑制剂活性及结构的影响  

Effect of Simulated Gastric Digestion in vitro on Activity and Structure ofα-Amylase Inhibitor in White Kidney Bean

作　　者：姜彩霞 郑喜群 刘晓兰[2,4] 王俊彤[2,3] 赵婉宏 曾祥瑞 Jiang Caixia;Zheng Xiqun;Liu Xiaolan;Wang Juntong;Zhao Wanhong;Zeng Xiangrui(National Coarse Cereals Engineering Center,Heilongjiang Bayi Agricultural University,Daqing 163319;Engineering Research Center of Processing and Utilization of Grain By-products and Utilization of Ministry of Education,Daqing 163319;College of Food Science,Heilongjiang Bayi Agricultural University,Daqing 163319;College of Food and Biological Engineering,Qiqihar University,Qiqihaer 161006)

机构地区：[1]黑龙江八一农垦大学国家杂粮工程技术中心,大庆163319 [2]粮食副产物加工与利用教育部工程研究中心,大庆163319 [3]黑龙江八一农垦大学食品学院,大庆163319 [4]齐齐哈尔大学食品与生物工程学院,齐齐哈尔161006

出　　处：《中国粮油学报》2023年第6期46-51,共6页Journal of the Chinese Cereals and Oils Association

基　　金：大庆市指导性科技计划项目(zd-2020-69);黑龙江八一农垦大学“三纵”基础培育项目(ZRCPY202007)。

摘　　要：为探究体外模拟胃部消化对α-淀粉酶抑制剂(α-AI)活性和结构特征的影响,实验以白芸豆为原料制备α-AI,探究体外模拟胃部消化不同时间产物的活性、粒径分布、Zeta电位、二级结构,以及巯基和二硫键含量。白芸豆中α-AI的分子质量约为34 ku,当消化时间大于90 min时产物对α-淀粉酶的抑制活性显著增加(P<0.05),粒径和Zeta电位绝对值显著降低(P<0.05);β-转角相对含量增加,无规则卷曲相对含量降低,总巯基、游离巯基含量均显著降低,二硫键含量显著升高。研究结果表明,体外模拟胃部消化过程中,白芸豆α-AI蛋白分子间的交互和聚集现象不断加剧,部分巯基发生氧化现象形成二硫键,形成稳定的蛋白质构象,能够在体内较好地发挥其抑制α-淀粉酶的活性。To explore the inhibitory activity and structural characteristics ofα-amylase inhibitors(α-AI)under the simulated gastric digestion in vitro,white kidney beans was used as the raw materials to prepareα-AI.Its inhibitory activity,particle size distribution,Zeta potential,secondary structure,sulphydryl and disulfide bond contents of the products were measured during the simulated digestion in vitro.The results indicated that the molecular weight ofα-AI from white kidney beans was 34 ku,the inhibitory activity of the product onα-amylase increased significantly after the digestion time was longer than 90 min(P<0.05),however,the particle size and absolute value of Zeta potential were reduced significantly(P<0.05);after simulated gastric digestion,it was found that the relative content ofβ-turn was increased,and the relative content of random curls was decreased,the content of total sulfhydryl groups and free sulfhydryl groups were reduced significantly,and the content of disulfide bonds increased significantly in theα-AI from white kidney beans.The results indicated that the interaction and aggregation of white kidney beanα-AI protein molecules continued to intensify,and some sulphydryl groups were oxidized to form disulfide bonds during the simulated gastric digestion in vitro,forming a stable protein conformation,which could better exert its activity of inhibitingα-amylase in the body.

关 键 词：白芸豆 Α-淀粉酶抑制剂 模拟消化 二级结构 

分 类 号：TS214.9[轻工技术与工程—粮食、油脂及植物蛋白工程]