高静压处理对醇变性大豆11S球蛋白影响研究

Effect of high hydrostatic pressure on ethanol-denatured soybean 11S globulin

研究了高静压处理对醇变性大豆11S球蛋白溶解性及结构性质的影响。结果表明,大豆11S球蛋白以1:15的比例添加65%乙醇处理后溶解度降低为14.24%。利用300 MPa高静压处理醇变性大豆11S球蛋白,可使其溶解度恢复至95.5%。凝胶渗透色谱显示,醇变性大豆11S球蛋白在不同高静压下形成多种相对分子质量的可溶性聚集体。荧光光谱和圆二色谱对高静压处理的醇变性大豆11S球蛋白结构的测定证实其结构逐步被打开,形成柔性三级结构;醇诱导稳定的α-螺旋结构部分被破坏,高静压处理后蛋白的二级结构以β-折叠为主。

Effects of high hydrostatic pressure （HHP） on the solubility and structure of ethanol - denatured soybean 11 S globulin were investigated. Soybean 11S globulin was denatured by 65 % ethanol with ratio of 1： 15. The solubility of ethanol - denatured soybean 11S globulin was 14.24% , and 300 MPa HHP treatment improved significantly its solubility to 95.5%. Gel permeation chromatograph showed that soluble - aggregations of various relative molecular weights were formed at different pressure. The analysis of fluorescence and circular dichroism spectra indicated that the structure of ethanol - denatured soybean 11S globulin was partially unfolded by HHP treatment, and flexible tertiary structure was found;the α - helix induced by ethanol was partially broken, and the secondary structure was mainly composed of β - sheet.