不同品种大豆分离蛋白结构与表面疏水性的关系  

Relationship between Structure and Surface Hydrophobicity of Soybean Protein Isolates from Different Varieties

作　　者：王辰[1] 江连洲[1,2] 魏冬旭[1,3] 李杨[1] 隋晓楠[1] 王中江[1,2] 李丹[1,4] 

机构地区：[1]东北农业大学食品学院,黑龙江哈尔滨150030 [2]国家大豆工程技术研究中心,黑龙江哈尔滨150030 [3]黑龙江出入境检验检疫局,黑龙江哈尔滨150001 [4]宁德师范学院生物工程,福建宁德352100

出　　处：《食品科学》2012年第9期54-57,共4页Food Science

基　　金：国家自然科学基金项目(31071493)

摘　　要：采用傅里叶变换红外光谱法(FTIR)对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进行研究。对不同品种大豆分离蛋白在酰胺Ⅰ带位置中各个特征峰相互叠加,采用Gauss峰型进行拟合、解析,判断其α-螺旋、β-折叠、β-转角和无规则卷曲的相对含量,对其含量与表面疏水性数值之间的关系进行分析,为研究大豆分离蛋白结构与表面疏水性之间的构效关系提供理论基础。结果表明:大豆分离蛋白表面疏水性与α-螺旋含量呈负相关(r=-0.945,P=0.004),与β-折叠(r=0.904,P=0.013)及无规则卷曲(r=0.866,P=0.026)的含量呈正相关,与β-转角线性关系不明显(r=-0.698,P=0.123)。FTIR（fourier transform infra-red spectroscopy） was applied to explore the secondary structure of soybean protein isolates from different varieties.The overlapped peaks of amide Ⅰof soy protein isolates from different species could be fitted by Gauss peak to reveal the characteristic peaks ofα-helix,β-sheet,β-turn and random coil.Their contents and surface hydrophobicity were determined to explore the structure-activity relationship of soybean protein isolates.The results revealed a good negative correlation between the surface hydrophobicity and α-helix content（r =-0.945,P = 0.004）,and a positive correlation between the surface hydrophobicity and β-sheet（r = 0.904,P = 0.013） or random coil content（r = 0.866,P =0.026）.No significant correlation between β-turn and the surface hydrophobicity（r =-0.698,P = 0.123）.

关 键 词：大豆分离蛋白 FTIR 表面疏水性 

分 类 号：TS201.21[轻工技术与工程—食品科学]