【作者】 王辰； 江连洲； 魏冬旭； 李杨； 李丹； 王中江；

【Author】 WANG Chen~a JIANG Lian-zhou~(a,b*) WEI Dong-xu~(a,c) LI Yang~a LI Dan~(a,d) WANG Zhong-jiang~a (a Northeast Agriculture University,Harbin 150030,China; b National Research Center of Soybean Engineering and Technology,Harbin 150030,China; c Heilongjiang Entry-exit Inspect and Quarantine Bureau,Harbin 150030,China; d Ningde Normal University,Ningde 352100,China)

【机构】 东北农业大学； 国家大豆工程技术研究中心； 黑龙江出入境检验检疫局； 宁德师范学院；

【摘要】 本实验旨在采用圆二色性光谱及拉曼光谱研究不同品种大豆分离蛋白的二级结构与表面疏水性之间的关系。首先对不同品种大豆分离蛋白的溶解度及表面疏水性进行测定,对大豆分离蛋白的二级结构进行定量分析,通过分析二者之间的数值规律进而研究了大豆分离蛋白二级结构与表面疏水性之间的构效关系。结果表明:不同品种大豆分离蛋白的溶解性、表面疏水性及二级结构存在较大差异,表面疏水性值随着α-螺旋含量降低而增大,随着β-折叠及无规则卷曲含量升高而减小,与β-转角含量变化无明显关系。即表面疏水性与α-螺旋含量呈现负相关,与β-折叠及无规则卷曲含量呈现正相关,与β-转角含量线性关系不显著。通过本实验对大豆分离蛋白表面疏水性的研究,为解决大豆分离蛋白在肉制品生产中分散不良的现象以及专一性大豆分离蛋白的开发奠定了理论基础。更多还原

【Abstract】 The circular dichroism spectra and Raman spectroscopy were accepted to study on the relationship between secondary structure and surface hydrophobicity in different varieties of soy protein isolate. First,the solubility and surface hydrophobicity of the different varieties of soybean protein isolate were measured,and the secondary structure of soybean protein isolates was analyzed quantitatively.By analyzing the difference of the values between the surface hydrophobicity and the secondary structure to study the structure-activity relationship between secondary structure and surface hydrophobicity of soybean protein isolate.The results showed that:the surface hydrophobicity increased with the decrease ofα-helix content, and decreased with the increase ofβ-sheet and random coil content,and the linear relationship betweenβ-turn content and the surface hydrophobicity was not significant.The study of the surface hydrophobicity of soy protein isolate has laid theoretical foundations for sovling the poor dispersion phenomenon of the soybean protein isolate in meat production and the development of the specific functional soybean protein isolate.更多还原