物理作用力对大豆分离蛋白乳化性及乳化稳定性的影响  

Effect of Physical Force on Emulsion Activity Index and Stability of Soybean Protein Isolate

作　　者：周荧[1] 黄行健[1] 吕思伊[1] 卢琪[1] 潘思轶[1] 

机构地区：[1]华中农业大学食品科学技术学院,湖北武汉430070

出　　处：《食品科学》2010年第7期71-74,共4页Food Science

基　　金：湖北省重点科技专项项目(2006AA201B29);国家"863"计划项目(2006AA10Z330)

摘　　要：研究物理作用力对4种供试大豆分离蛋白乳化性及乳化稳定性的影响。分别采用不同浓度的NaCl、NaSCN、尿素和1,2-丙二醇处理大豆分离蛋白以改变其物理作用力。研究结果表明:随着NaCl和NaSCN浓度的增加,乳化活性指数(EAI)值均呈先降低再升高的趋势,说明静电作用力起主导作用,疏水相互作用不利于乳化性。随着NaCl和NaSCN浓度的升高,乳化稳定性(ES)值均降低,说明静电作用力起主导作用,并且比疏水相互作用力的影响强。加入尿素可使蛋白质的疏水基团暴露出来,使EAI值升高,但是加入不同浓度的尿素对乳化性的影响差别不大。EAI值随着1,2-丙二醇浓度的升高而升高,说明氢键相互作用利于乳化活性和乳化稳定性。To under the effect of physical force on emulsion activity index（EAI） and emulsifying stability（ES） of soybean protein isolates（SPIs） obtained from different varieties of soybeans,various concentrations of NaCl,NaSCN,urea and 1,2-propylene were respetively used to treat SPI for changing its physical force.Results indicated that the increasing concentration of NaCl and NaSCN resulted in an initial increase and a following reduction of EAI of SPI.This suggests that electrostatic interaction was a dominant force and hydrophobic interaction is unfavorable to EAI of SPI.The fact that emulsifying stability was decreased with increasing concentrations of NaCl and NaSCN demonstrates that electrostatic interaction is stronger than hydrophobic interaction.The addition of urea improved the exposure of hydrophobic groups in protein and promoted the increase of EAI of SPI.However,no obvious effect of added urea at different levels on EAI was observed.Furthermore,as 1,2-propylene concentration increased,there was an increase of EAI.Therefore,hydrogen bonding interactions are beneficial to EAI and ES of SPI.

关 键 词：大豆分离蛋白 静电相互作用 疏水相互作用 乳化性 乳化稳定性 

分 类 号：Q51[生物学—生物化学]