牦牛β-乳球蛋白分离纯化及在不同pH值温度的变性研究

Research of separate Yak β-Lactoglobulin and denaturation at different pH and heating temperature

通过采用反向液相色谱(RP-HPLC)对不同方法分离乳清蛋白的结果进行分析,同时检测分离纯化的牦牛β-乳球蛋白进行,其蛋白纯度达到90%以上。另外使用非变性凝胶电泳(Native-PAGE)对不同pH值、不同加热温度条件下牦牛β-乳球蛋白的变性条件及变性进行了研究。结果表明,牦牛β-乳球蛋白的变性温度在80℃左右。蛋白变性含量随着加热温度和pH值的增加成上升趋势。加热至90℃后蛋白变性质量分数增加显著在pH6和pH9条件下未变性蛋白质量分数分别为24%和9%。

Yak whey protein obtained by different methods analyzed by RP-HPLC. The purity of separation β-1actoglobulin was more than 90%. Using Native-PAGE to detected the condition and content of yak/3-1actoglobulin denaturation at different pH （6.0 to 9.0）and heating temperature（60 to 90 ℃）. The results shown that the denaturation of β-lactoglobulin was about 80 ℃, and the content of denaturation/8-1actoglobulin was increased with pH and heating temperature increased. With heating temperature to 90 ℃ , the content of native β-1actoglobulin was 24% and 9% at pH6.0 and pH9.0 respectively.