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pH 值对大豆分离蛋白构象及表面疏水性的影响
引用本文:王中江,江连洲,魏冬旭,李杨,王辰,李丹.pH 值对大豆分离蛋白构象及表面疏水性的影响[J].食品科学,2012,33(11):47-51.
作者姓名:王中江  江连洲  魏冬旭  李杨  王辰  李丹
作者单位:1.东北农业大学食品学院 2.国家大豆工程技术研究中心 3.黑龙江出入境检验检疫局 4.宁德师范学院
基金项目:国家自然科学基金项目(C200101)
摘    要:采用Lowery法、ANS荧光探针法、圆二色光谱、荧光光谱方法分别对不同pH值大豆分离蛋白溶解度、表面疏水性、蛋白质二级、三级结构进行分析。结果表明:随着pH值的升高,大豆分离蛋白的二级结构发生由β-折叠结构向α-螺旋结构的转变,其Trp残基所处微环境极性增强。大豆分离蛋白表面疏水性与溶解度呈负相关关系,同时大豆分离蛋白表面疏水性也与α-螺旋结构含量呈负相关关系。

关 键 词:大豆分离蛋白  pH值  表面疏水性  构象  

Effect of pH on Conformation and Surface Hydrophobicity of Soybean Protein Isolate
WANG Zhong-jiang,JIANG Lian-zhou,WEI Dong-xu,LI Yang,WANG Chen,LI Dan.Effect of pH on Conformation and Surface Hydrophobicity of Soybean Protein Isolate[J].Food Science,2012,33(11):47-51.
Authors:WANG Zhong-jiang  JIANG Lian-zhou  WEI Dong-xu  LI Yang  WANG Chen  LI Dan
Affiliation:(1. College of Food Science, Northeast Agricultural University, Harbin 150030, China;2. National Soybean Engineering Technology Research Center, Harbin 150030, China;3. Heilongjiang Entry-Exit Inspection and Quarantine Bureau, Harbin 150001, China; 4. Ningde Normal University, Ningde 352100, China)
Abstract:Lowry method,ANS fluorescence probe,circular dichroism and fluorescent spectroscopy were applied to explore the solubility,surface hydrophobicity,secondary structure and tertiary structure of soybean protein isolate at different pH conditions.The results showed that the transformation from β-sheet structure to α-helix structure,and the microenvironment polarity of Trp residues revealed an obvious increase with increasing pH.A negatively linear correlation between the surface hydrophobicity and solubility of soybean protein isolate was observed.Meanwhile,the surface hydrophobicity of soybean protein isolate was negatively correlated with the amount of α-helix structure.
Keywords:soybean protein isolate  pH  hydrophobicity  structure
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