摘要
采用荧光法研究了十二烷基三甲基氯化铵(dodecyl-trimethyl ammonium chloride,DTAC)反胶束Wo值对萃取蛋白质乳化性影响的机理。结果表明,随着反胶束Wo值的增大,萃取蛋白质的结构会发生变化,表面疏水性随之增加,从而蛋白质的乳化活性略微下降,乳化稳定性显著增大。萃取蛋白质的表面疏水性与乳化活性显著负相关,与乳化稳定性显著正相关。
The influence of Wo of dodecyl-trimethyl ammonium chloride（DTAC）reverse micelles on proteinextracted was investigated by fluorescence method. The results showed that with the water content of reversemicelles increased,the structure of protein extraction changed,and surface hydrophobicity increased.Emulsifying activity of protein declined slightly,emulsion stability increased significantly. There wasasignificant negative correlation between surface hydrophobicity and emulsifying activity,and a significantpositive correlation between surface hydrophobicity and emulsifying stability.
出处
《食品研究与开发》
CAS
北大核心
2018年第5期42-47,共6页
Food Research and Development
基金
2014年度河南省高等学校青年骨干教师培养计划(2014GGJS-197)
关键词
蛋白质
乳化性
表面疏水性
反胶束
DTAC
protein
emulsifying properties
surface hydrophobicity
reverse micelles
DTAC
