摘要
以白芸豆为原料,采用酶解法制备α-淀粉酶抑制剂肽。在单因素试验的基础上,采用响应面试验优化制备工艺,并采用紫外光谱和红外光谱表征其结构。结果表明:酸性蛋白酶在pH为2.5时酶解效果最好,最佳酶解工艺条件为酶添加量5 500 U/g(以白芸豆蛋白粉质量计)、酶解时间1.5 h、酶解温度30℃,在此条件下白芸豆多肽α-淀粉酶抑制剂肽对α-淀粉酶抑制率为59.09%;紫外光谱在270~300 nm处有最高吸收峰,表明多肽含有芳香族氨基酸色氨酸(Trp)和酪氨酸(Tyr);红外光谱扫描表明,白芸豆α-淀粉酶抑制剂肽的二级结构中63.80%为β-折叠构象。
Using white kidney bean as the raw material,α-amylase inhibitor peptides were prepared by enzymatic hydrolysis.Based on single-factor experiments,the preparation technology was optimized by response surface methodology.The structure of the peptides was characterized by UV and FT-IR spectroscopy.The results showed that acidic protease had the best enzymatic hydrolysis effect at pH 2.5.The optimal enzymatic hydrolysis conditions were enzyme addition 5500 U/g(based on the mass of white kidney bean protein powder),enzymatic hydrolysis time 1.5 h,and enzymatic hydrolysis temperature 30℃.Under these conditions,the inhibition rate of white kidney bean peptide onα-amylase was 59.09%.The UV spectrum showed the highest absorption peak at 270-300 nm,indicating that the peptide contains aromatic amino acids such as tryptophan(Trp)and tyrosine(Tyr).IR spectroscopy scanning showed that the secondary structure of the white kidney beanα-amylase inhibitor peptide was mainlyβ-folded conformation,accounting for 63.80%.
作者
唐衍洲
刘聪
尹乐斌
黄秋萍
朱芊芊
谭文慧
TANG Yanzhou;LIU Cong;YIN Lebin;HUANG Qiuping;ZHU Qianqian;TAN Wenhui(School of Food and Chemical Engineering,Shaoyang University,Shaoyang 422000,Hunan,China;Shaoyang Industrial Vocational and Technical College,Shaoyang 422000,Hunan,China;Key Laboratory of Soybean Product Processing and Safety Control in Hunan Province,Shaoyang 422000,Hunan,China)
出处
《粮食与油脂》
北大核心
2026年第1期140-146,共7页
Cereals & Oils
基金
湖南省自然科学基金项目(2023JJ50261)
湖南省普通高等学校科技创新团队支持项目(湘教通[2023]233号)
邵阳学院研究生科研创新项目(CX2024SY011)
邵阳学院横向项目(2024HX119)
邵阳市科技计划项目(2025PT4054)。
关键词
白芸豆
Α-淀粉酶抑制剂
结构表征
white kidney bean
α-amylase inhibitor
structural characterization
