α和α′亚基缺失对大豆分离蛋白乳化特性的影响  

Effects of the subunit-deficiency ofαandα′on emulsifying properties of soy protein isolate

作　　者：孙贺 于寒松[1,3] 范宏亮 付洪玲 单单单 吕博 宋波 刘珊珊[2] Sun He;Yu Hansong;Fan Hongliang;Fu Hongling;Shan Dandan;Lyu Bo;Song Bo;Liu Shanshan(College of Food Science&Engineering,Jilin Agricultural University,Changchun 130118,China;College of Agriculture,Northeast Agricultural University,Harbin 150030,China;Division of Soybean Processing,Soybean Research&Development Center,Chinese Agricultural Research System,Changchun 130118,China;College of Food Science,Northeast Agricultural University,Harbin 150030,China)

机构地区：[1]吉林农业大学食品科学与工程学院,长春130118 [2]东北农业大学农学院,哈尔滨150030 [3]国家大豆产业技术体系加工研究室,长春130118 [4]东北农业大学食品学院,哈尔滨150030

出　　处：《农业工程学报》2020年第10期261-268,共8页Transactions of the Chinese Society of Agricultural Engineering

基　　金：国家大豆产业技术体系(CARS-04)。

摘　　要：为了探究β-伴大豆球蛋白(7S)中α和α′亚基缺失对大豆分离蛋白乳化特性的影响,该文以东农47(对照)和3种不同蛋白亚基缺失型(α缺失、α′缺失以及α、α′缺失)大豆为原料提取大豆分离蛋白(Soy Protein Isolate,SPI),通过十二烷基磺酸钠聚丙烯酰胺凝胶电泳(Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis,SDS-PAGE)技术分析其亚基组成,然后制备乳状液并测定乳化活性指数(Emulsifying Activity Index,EAI)、ζ-电位、粒径、微观结构、稳定动力学指数(Turbiscan Stability Index,TSI)及界面蛋白吸附量。结果表明:α′亚基缺失型SPI乳状液乳化活性指数最大,为87.59 m^2/g;ζ-电位绝对值最大,为47.7 mV;粒径最小,为2.223μm;显微结构显示其分子最小且分布最均匀,稳定动力学指数最小;界面蛋白吸附量最大,为31.40%。4种不同SPI乳状液的稳定性结果由大到小为α′亚基缺失型、东农47、α亚基缺失型、α和α′亚基缺失型。研究结果可为高乳化性大豆蛋白系列产品的开发应用提供理论支撑和技术支持。Soybean protein is one of the major plant-derived protein resources due to its high yield and a wide range of processing applications.It is necessary to effectively improve processing properties of soybean protein,and thereby significantly enhance its nutritional value and economic potency.Most previous research mainly focused on the effects of external physical or chemical conditions and other complex system on the processing parameters of soybean protein.Few studies developed to explore the effect of various subunits compositions on the processing properties of soybean protein,particularly lacking on the deficiency of small subunit.Therefore,this study aims to investigate the effects ofαandα′subunits inβ-conglycinin on emulsifying properties of soybean protein.In the experiment,some raw materials include Dongnong 47 and three different protein subunit-deficiency(αsubunit-deficiency,α′subunit-deficiency andα′,αsubunit-deficiency)soybeans,to extract the soy protein isolates(SPI),by using the method of alkali solution acid precipitation for the preparation of emulsion.The subunit composition was then analyzed by sodium dodecyl sulfonate polyacrylamide gel electrophoresis(SDS-PAGE).Some parameters,including emulsifying activity index(EAI),ζ-potential,particle size,microstructure,turbiscan stability index(TSI),and interface adsorbed protein,were selected to evaluate the effect ofαandα′subunits inβ-conglycinin(7S)on emulsifying properties of soy protein isolate.The results showed that the soy protein isolate emulsion ofα′subunit-deficiency has the highest emulsifying activity index(87.59 m2/g),the maximumζ-potential absolute(47.7 mV),the minimum particle size(2.223μm),the smallest molecules and most evenly distributed through the analysis of microstructure,the smallest turbiscan stability index(TSI),and the maximum content of interface adsorbed protein(31.40%),compared with other two SPI.The emulsion stability of soy protein isolate ranked in order:α′subunit-deficiency,Dongnong 47,αsubunit

关 键 词：乳化活性 乳化稳定性 微观结构 大豆分离蛋白 亚基缺失型 

分 类 号：TS214.2[轻工技术与工程—粮食、油脂及植物蛋白工程]