高压处理对牛骨骼肌G-肌动蛋白结构的影响  

Effect of High-pressure Treatment on G-actin Structure of Bovine Skeletal Muscle

作　　者：王志峰[1] 包.格日勒图 

机构地区：[1]内蒙古农业大学食品科学与工程学院,内蒙古呼和浩特010018

出　　处：《食品科学》2010年第13期6-9,共4页Food Science

基　　金：国家自然科学基金项目(20676058)

摘　　要：从牛骨骼肌中提取G-肌动蛋白,并用0.1～400MPa高压处理,对G-肌动蛋白的荧光光谱、质量中心、表面巯基含量、芳香族表面疏水性残基的变化进行分析,探讨G-肌动蛋白的结构变化。在0.1～100MPa处理时G-肌动蛋白荧光强度呈下降趋势,在200～400MPa处理时荧光强度呈上升趋势,荧光强度峰值的极大波长发生蓝移。100MPa压力下G-肌动蛋白质量中心稍微下降,但压力在100～300MPa时质量中心呈上升趋势。表面巯基含量随着压力的增高有明显上升趋势。随着压力的升高芳香族表面疏水性残基的荧光强度升高,压力为300MPa时显示最高值。从此结果可推测超高压处理引起的G-肌动蛋白三级结构变化是不可逆变化。G-actin was prepared from bovine skeletal muscle and exposed to pressures ranging from 0.1 to 400 MPa. The high pressure-induced structural change of G-actin was explored in terms of fluorescence spectrum, center of spectral mass, the amount of surface sulfhydryl （SH） group and surface aromatic hydrophobicity. The fluorescence intensity of G-actin decreased as pressure increased from 0.1 to 100 MPa; however, an opposite change was observed as pressure increased from 200 to 400 MPa; and the fluorescence spectrum of G-actin exhibited a blue shift due to exposure to higher pressures. As pressure increased from 100 to 300 MPa, the center of spectral mass of G-actin initially decreased slightly, reaching its minimum value at 100 MPa, followed by a rebound increase, and the amount of surface sulfhydryl group gradually increased, and the surface aromatic hydrophobicity changed in a manner similar to that of the amount of surface sulfhydryl group, reaching its maximum value at 300 MPa. Therefore, high pressure-induced three-dimensional structural change of G-actin might be irreversible.

关 键 词：高压处理 G-肌动蛋白 质量中心 巯基 芳香族表面疏水性 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]