米胚蛋白组分的提取及功能性质研究  

Extraction of rice germ protein components and their functional properties

作　　者：李捷[1] 熊华[1] 史苏华[1] 蒋岩[1] 杜研学[1] 张忠[1] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,南昌330047

出　　处：《食品科技》2012年第1期155-159,共5页Food Science and Technology

基　　金：国家发改委项目(发改投资[2009]2825号);南昌大学食品科学与技术国家重点实验室目标导向项目(SKLF-MB-201005)

摘　　要：采用Osborne的方法,从米胚中提取清蛋白、球蛋白、醇溶蛋白和谷蛋白,4种蛋白中谷蛋白的含量最高,占72.69%,其余3种蛋白的含量相差不大;考察4种蛋白的溶解性得出,在pH5下4种蛋白的溶解性最低,随着pH的增大或减小,溶解性逐渐增加,且清蛋白和球蛋白的溶解性较醇溶蛋白和谷蛋白高;在pH11、0.1mol/L NaCl浓度、1mg/mL蛋白浓度下,加入3mL大豆油,4种蛋白的乳化活性及乳化稳定性均达到最大值。Albumin, globulin, prolamin and glutelin were extracted from rice germ by the method of Osborne. The amount of glutelin was the highest among the four protein fractions, which accounted for 72.69%. And the amounts of the other three protein fractions were nearly the same. The solubilities of the four protein fractions were investigated and the results indicated that the solubilities of all protein fractions were the lowest at pH5, and it would increase with the pH increasing. Compared to prolamin and glutelin, the solubility of albumin and globulin were higher. The emulsifying and emulsion stabilities of all four protein fractions reached the highest under the condition of pH11, 0.1 mol/L NaCl and 1 mg/mL protein concentration.

关 键 词：米胚蛋白 溶解性 乳化性 

分 类 号：TS201.21[轻工技术与工程—食品科学] TS210.9[轻工技术与工程—食品科学与工程]