Effect of secondary structure determined by CD spectra on surface hydrophobicity of soybean protein isolate
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摘要: 旨在采用圆二色性光谱手段研究二级结构对我国六种经常使用的大豆品种制备而成的分离蛋白的表面疏水性的影响。实验先是对六个品种的大豆进行分离蛋白的提取,并对其性质进行测定,包括溶解度和表面疏水性;再对六种大豆分离蛋白的二级结构进行测定和分析;通过SPSS软件对六种大豆分离蛋白的表面疏水性和二级结构的数值进行线性相关性分析,探究二者之间的构效关系。研究中发现六个品种的大豆分离蛋白的二级结构、溶解性、表面疏水性都差异显著（p<0.05）,表面疏水性的大小随着α-螺旋含量升高而减小,随着无规则卷曲和β-折叠含量增大而提高,因β-转角含量变化的影响不明显。SPSS线性相关性分析表明品种间的表面疏水性与β-转角含量线性关系不显著,与无规则卷曲、β-折叠含量呈正向相关,与α-螺旋含量呈负向相关。Abstract: CD( circular dichroism spectra) was applied to research on the relationship between surface hydrophobicity( SH) and secondary structure in six varieties of soy protein isolate( SPI). First step was the extraction of SPIs,the functional abilities( surface hydrophobicity and solubility) and the secondary structure of the six varieties of SPI were measured and analyzed.Through SPSS software,the numerical linear correlation bewteen surface hydrophobicity and secondary structure of six varieties of soybean protein isolate was analyzed to explore the structure- activity relationship between them. The results revearled that there were significant differences( p < 0.05) bewteen the secondary structure and the functional abilities( surface hydrophobicity and solubility).The SH of the six varieties of SPI increased with the decrease of α- helix content,and decreased with the increase of random coil and β-sheet content,and the linear relationship between the SH and β-turn content was not obvious. SPSS linear correlation analysis showed that the SH of the six varieties of SPI had no significant linear relationship with β-turn content,positively related to random coil and β-sheet content,and negative correlated to α-helix content.
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Keywords:
- soybean protein isolate /
- surface hydrophobicity /
- circular dichroism
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