中文摘要：

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）。

英文摘要：

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）.