摘要
对不同品种大豆分离蛋白(soybean protein isolate,SPI)的表面疏水性、氨基酸组成及溶液的Zeta电位和粒径分布进行分析,探讨蛋白质溶液Zeta电位和粒径分布与表面疏水性的关系。不同品种SPI的表面疏水性由大到小的变化趋势为:东农46>皖豆24>黑农46>五星4>中黄13>冀NF58,品种差异对SPI的Zeta电位及粒径分布具有显著影响。相关性分析表明,SPI表面疏水性与氨基酸组成无显著相关性,表面疏水性与Zeta电位绝对值呈显著的正相关,与粒径大小呈显著的负相关。当蛋白溶液Zeta电位绝对值较大时,蛋白表面更多同性电荷间的排斥作用会减少蛋白分子的相互聚集,使蛋白溶液趋于稳定,同时降低蛋白质粒径大小。此时,蛋白质疏水基团的内卷程度降低,并更多暴露在分子表面,导致蛋白质表面疏水性增加。
This study was done with the objective to analyze the surface hydrophobicity, amino acid composition, zeta potential and particle size distribution of soybean protein isolates (SPIs) prepared from different soybean varieties and to explore the relationship between surface hydrophobicity and zeta potential as well as particle size distribution of SPI. The surface hydrophobicity of SPIs from different varieties was in the decreasing order: Dongnong 46 > Wandou 24 > Heinong 46 > Wuxing 4 > Zhonghuang 13 > Ji NF 58. The different varieties had a significant effect on the zeta potential and particle size distribution of SPI. Correlation analysis indicated no significant correlation between surface hydrophobicity and amino acid composition. Surface hydrophobicity was positively correlated with absolute value of zeta potential and negatively correlated with particle size. With increasing absolute value of zeta potential, the aggregation of protein molecules was decreased due to repulsive interaction of more like electric charges on their surface, making the protein solution more stable and at the same time reducing the size of the protein particles. As a result, more hydrophobic groups were exposed on the surface of the proteins due to decreased involution degree of hydrophobic groups, thereby leading to an increase in surface hydrophobicity.
作者
齐宝坤
李杨
王中江
隋晓楠
江连洲
QI Baokun;LI Yang;WANG Zhongjiang;SUI Xiaonan;JIANG Lianzhou(College of Food Science, Northeast Agricultural University, Harbin 150030, China)
出处
《食品科学》
EI
CAS
CSCD
北大核心
2017年第3期114-118,共5页
Food Science
基金
国家现代农业产业技术体系建设专项(CARS-04-PS25)
关键词
大豆分离蛋白
ZETA电位
粒径分布
表面疏水性
soybean protein isolate
zeta potential
particle size distribution
surface hydrophobicity
