蓝圆鲹骨骼肌GPI的纯化及其对肌原纤维降解的抑制  

Purification of Glucose-6-phosphate Isomerase and Its Inhibition on the Degradation of Myofibrillar Proteins from Blue Scad Skeletal Muscle

作　　者：张超群[1,2] 钟婵[1,2] 王诚[1,2] 苏文金[1,2] 曹敏杰[1,2] 

机构地区：[1]集美大学生物工程学院,福建厦门361021 [2]福建省高校水产科学技术与食品安全重点实验室,福建厦门361021

出　　处：《集美大学学报（自然科学版）》2012年第6期414-420,共7页Journal of Jimei University：Natural Science

基　　金：国家自然科学基金资助项目(20872049)

摘　　要：通过硫酸铵分级沉淀、Q-Sepharose阴离子交换层析和SP-Sepharose阳离子交换层析等方法,从蓝圆鲹骨骼肌中分离纯化得到葡萄糖-6-磷酸异构酶(GPI).SDS-PAGE结果显示,GPI分子质量约为56 ku;Western-blot分析显示,纯化的蛋白质与抗白姑鱼GPI多克隆抗体有很强的阳性反应,表明其为GPI;GPI的最适pH值和最适温度分别为8.0和40℃;GPI能有效抑制蓝圆鲹肌原纤维蛋白在55℃下的自身降解,且随着GPI添加浓度的增加,肌原纤维蛋白的降解逐渐受到抑制,提示GPI可用于鱼糜制品生产以提高产品的凝胶强度.Glucose-6-phosphate isomerase （GPI） from the blue scad skeletal muscle was purified to homogeneity by ammonium sulfate fractionation, column chromatographies of Q-Sepharose and SP-Sepharose. Purified GPI revealed a single band on SDS-PAGE with molecular weight of 56 ku. Western-blot analysis revealed that the purified protein from blue scad reacted positively with the polyclonal antibody against GPI from white croaker, suggesting this protein was GPI. The optimum pH and temperature of blue scad GPI were 8.0 and 40 ℃, respectively. At 55 ℃, with the increasing addition of GPI, the degradation of myofibrillar proteins was effectively inhibited, suggesting GPI could be applied for surimi production in order to improve the elasticity of the product.

关 键 词：葡萄糖-6-磷酸异构酶 蓝圆鲹 纯化 降解 抑制 肌原纤维 

分 类 号：Q558[生物学—生物化学]