DHPM协同胃蛋白酶对β-乳球蛋白构象的影响  

Effect of DHPM and Pepsin on the Structure of β-Lactoglobulin

作　　者：洪启通 钟俊桢[1] 俞宏达[1] 刘成梅[1] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,南昌330047

出　　处：《中国食品学报》2017年第10期51-56,共6页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家自然科学基金项目(21366021)

摘　　要：采用动态高压微射流(DHPM)协同胃蛋白酶处理β-乳球蛋白,使用圆二光谱及荧光等方式研究β-乳球蛋白二三级构象的变化。研究发现DHPM协同胃蛋白酶处理过程中β-乳球蛋白构象变化与胃蛋白酶作用时间存在密切关联。当压力由0.1 MPa增至80 MPa时,DHPM协同胃蛋白酶处理能显著提高β-乳球蛋白的-SH含量,而蛋白质的表面疏水性减弱,二级结构以及氨基酸三维空间构象暴露程度发生变化,且同一压力下随着胃蛋白酶酶解时间的延长,β-乳球蛋白构象的变化更加显著。这些变化说明DHPM作用下促进了β-乳球蛋白和胃蛋白酶的相互作用,导致蛋白质构象发生显著变化。The changes of β-lactoglobulin secondary and tertiary conformation,treated by pepsin combined with dynamic high pressure microfluidization（DHPM）,were investigated by circular dichroism spectra and fluorescence spectra.The results showed that there was a close relationship between β-lactoglobulin conformational changes and the reaction time of pepsin after dynamic high pressure microfluidization（DHPM） treatment.When the pressure increased from 0.1 MPa to 80 MPa,the SH content of β-lactoglobulin increased significantly,surface hydrophobicity decreased and the exposure degree of secondary structure and the three-dimensional conformation of amino acids changed in a certain extent.While the conformation of β-lactoglobulin changed more remarkable with the reaction time of peps inincreasing in the same pressure.These results indicated that the interaction between β-lactoglobulin and pepsin was promoted under DHPM treatment,resulting in significant changes of protein conformation.

关 键 词：Β-乳球蛋白 动态高压微射流 胃蛋白酶 构象 

分 类 号：TS201.21[轻工技术与工程—食品科学]