牛背最长肌高铁肌红蛋白还原酶的分离及其酶学性质

Purification and characterization of metmyoglobin reductase in beef longissimus muscle

以冷鲜牛背最长肌为原料,采用硫酸铵盐析、超滤法对原料肉中的高铁肌红蛋白还原酶进行粗分离,并研究温度、pH、金属离子对高铁肌红蛋白还原酶活性的影响。结果表明:在硫酸铵饱和度65%,超滤(>50kDa)条件下,牛背最长肌高铁肌红蛋白还原酶可得到分离与纯化。试验范围内,牛背最长肌高铁肌红蛋白还原酶的分子量为29.0~66.4kDa,适宜温度为40℃,pH为6.0,Cu2+可明显抑制牛背最长肌高铁肌红蛋白还原酶活性。

The longissimus muscle from chilled beef was used as raw material to preliminary study the purification and characteristics of metmyoglobin reductase.The effect of temperature,pH and metal ions on the metmyoglobin reductase activity was investigated.Results revealed that the metmyoglobin reductase of longissimus muscle could be crudely purified with ammonium sulfate(65%saturation)and ultrafiltration(>50 kDa).SDS-PAGE analysis showed that the molecular weight of the metmyoglobin reductase of longissimus muscle was 29.0~66.4 kDa,mainly.The proper temperature of the metmyoglobin reductase of longissimus muscle was 40℃,with the proper pH 6.0.Cu2+ could inhibit the activity of the metmyoglobin reductase obviously.