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大豆分离蛋白-花青素复合物的制备及其蛋白结构与功能性质分析
引用本文:江连洲,陈思,李杨,吴长玲,王中江,张巧智,齐宝坤,隋晓楠,陈复生,许振国.大豆分离蛋白-花青素复合物的制备及其蛋白结构与功能性质分析[J].食品科学,2018,39(10):20-27.
作者姓名:江连洲  陈思  李杨  吴长玲  王中江  张巧智  齐宝坤  隋晓楠  陈复生  许振国
作者单位:(1.东北农业大学食品学院,黑龙江?哈尔滨 150030;2.河南工业大学粮油食品学院,河南?郑州 450001;3.山东省高唐蓝山集团总公司,山东?聊城 252000)
基金项目:国家自然科学基金青年科学基金项目(31601475);国家自然科学基金面上项目(31671807); “十三五”国家重点研发计划重点专项(2016YFD0401402;2016YFD0400700)
摘    要:大豆分离蛋白经热处理后与花青素进行复合形成复合物,采用荧光光谱表征复合体系构象变化,以溶解性、乳化性、乳化稳定性、粒度分析及Zeta电位为指标分析该复合体系中大豆分离蛋白二级结构的变化与功能性质表达之间的关系。结果表明:在pH?7.4的条件下,热处理大豆分离蛋白与花青素复合后,大豆分离蛋白的Zeta电位绝对值显著增大,乳化性、乳化稳定性显著提高,但溶解性显著下降。通过荧光光谱分析发现花青素对热处理大豆分离蛋白的荧光猝灭机制为静态猝灭,蛋白与花青素间形成了结合位点数近似于1的复合物,三维荧光光谱结果表明花青素的复合使得蛋白质多肽链的骨架伸展,蛋白结构发生变化。

关 键 词:大豆分离蛋白  花青素  结构性质  功能性质  

Effects of Complexation with Anthocyanin on the Structural and Functional Properties of Denatured Soybean Protein
JIANG Lianzhou,CHEN Si,LI Yang,WU Changling,WANG Zhongjiang,ZHANG Qiaozhi,QI Baokun,SUI Xiaonan,CHEN Fusheng,XU Zhenguo.Effects of Complexation with Anthocyanin on the Structural and Functional Properties of Denatured Soybean Protein[J].Food Science,2018,39(10):20-27.
Authors:JIANG Lianzhou  CHEN Si  LI Yang  WU Changling  WANG Zhongjiang  ZHANG Qiaozhi  QI Baokun  SUI Xiaonan  CHEN Fusheng  XU Zhenguo
Affiliation:(1. College of Food Science, Northeast Agricultural University, Harbin 150030, China;2. College of Food Science and Technology, Henan University of Technology, Zhengzhou 450001, China;3. Shandong Gaotang Lanshan Group Corporation, Liaocheng 252000, China)
Abstract:This paper is focused on the effect of interaction with anthocyanin on the structure and function of denatured soybean protein. Fluorescence spectroscopy was used to study the conformational changes of the complexes. The relationship between structural change and functional properties was analyzed through determination of solubility, emulsifying ability, emulsifying stability, particle size analysis and Zeta potential analysis. The results showed that the absolute value of Zeta potential as well as emulsifying activity and emulsion stability of denatured soybean protein increased significantly after complexation with anthocyanin at pH 7.4, whereas its solubility decreased. The fluorescence spectra showed that the fluorescence quenching of heat-treated soybean protein by anthocyanin was a static quenching process with the formation of binding sites close to 1. The three dimensional fluorescence spectra indicated that complexation with anthocyanin extended the protein polypeptide backbone and changed the protein structures.
Keywords:soybean protein isolate  anthocyanin  structural property  functional property  
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