大豆蛋白的结构特性研究  

Study on structural properties of soybean protein isolate

作　　者：段春红[1] 孙婉[2] 姚晓琳[2] 韩晓红[1] 潘思轶[2] 

机构地区：[1]武汉生物工程学院,湖北武汉430415 [2]华中农业大学食品科技学院,湖北武汉430070

出　　处：《粮食与饲料工业》2010年第8期19-20,24,共3页Cereal & Feed Industry

基　　金：863项目(2006AA10Z330);湖北省新世纪高层次人才工程入选人员科研择优资助项目(鄂人[2003]31号)

摘　　要：以中豆36为原料,分别提取大豆分离蛋白(SPI)、7S、11S球蛋白,利用SDS-PAGE、SEM、表面疏水性和巯基含量的变化等手段考察了蛋白分子结构。结果表明:7S、11S和SPI结构存在差异;采用扫描电镜观察发现在同一放大倍数下,7S、11S球蛋白和SPI单体分子表面呈现不同性状;对其巯基及疏水性测定比较发现,SPI中游离巯基和总巯基含量均最高,其次是11S球蛋白,而7S球蛋白中游离巯基和总巯基含量较低;11S球蛋白具有较高的疏水性,而7S球蛋白的疏水性相对较低。In this study, soybean Zhongdou 36 was used as the raw material to extract soybean protein isolate （SPI）, 7S and 11S globulins; SDS PAGE, scanning electron microscope （SEM）, variations of surface hydrophobicity and the sulfhydryl content were applied to examine the structure of protein molecules. As seen from the results, there existed some difference in the structures of 7S, 11S and SPL As observed by the SEM, under the same enlargement magnitude, the surfaces of 7S, 11S globulin and SPI monomers presented different properties. As discovered from the detections of sulfhydryl content and hydrophobicity, free sulfhydryl and total sulfhydryl in SPI were both the highest, followed by llS globulin, while in 7S globulin were both the lowest. 11S globulin had higher hydrophobicity, and 7S globulin had lower.

关 键 词：大豆分离蛋白 7S球蛋白 11S球蛋白 结构特性 

分 类 号：TS201.2[轻工技术与工程—食品科学]