ALTERED ENZYMATIC ACTIVITY OF LYSOZYMES BOUND TO VARIOUSLY SULFATED CHITOSANS  

作　　者：袁琳 陈红 

机构地区：[1]Jiangsu Key Laboratory of Advanced Functional Polymer Design and Application,Department of Polymer Science and Engineering,College of Chemistry,Chemical Engineering and Materials Science,Soochow University

出　　处：《Chinese Journal of Polymer Science》2012年第6期893-899,共7页高分子科学（英文版）

基　　金：supported by the National Natural Science Foundation of China(Nos.20920102035,20974086, and 21074083);the Priority Academic Program Development of Jiangsu Higher Education Institutions(PAPD)

摘　　要：The purpose of this research is to investigate the effects of the variously sulfated chitosans on lysozyme activity and structure. It was shown that the specific enzymatic activity of lysozyme remained almost similar to the native protein after being bound to 6-O-sulfated chitosan （6S-chitosan） and 3,6-O-sulfated chitosan （3,6S-chitosan）, but decreased greatly after being bound to 2-N-6-O-sulfated chitosan （2,6S-chitosan）. Meanwhile, among these sulfated chitosans, 2,6S-chitosan induced the greatest conformational change in lysozyme as indicated by the fluorescence spectra. These findings demonstrated that when sulfated chitosans of different structures bind to lysozyme, lysozyme undergoes conformational change of different magnitudes, which results in corresponding levels of lysozyme activity. Further study on the interaction of sulfated chitosans with lysozyme by surface plasmon resonance （SPR） suggested that their affinities might be determined by their molecular structures.The purpose of this research is to investigate the effects of the variously sulfated chitosans on lysozyme activity and structure. It was shown that the specific enzymatic activity of lysozyme remained almost similar to the native protein after being bound to 6-O-sulfated chitosan （6S-chitosan） and 3,6-O-sulfated chitosan （3,6S-chitosan）, but decreased greatly after being bound to 2-N-6-O-sulfated chitosan （2,6S-chitosan）. Meanwhile, among these sulfated chitosans, 2,6S-chitosan induced the greatest conformational change in lysozyme as indicated by the fluorescence spectra. These findings demonstrated that when sulfated chitosans of different structures bind to lysozyme, lysozyme undergoes conformational change of different magnitudes, which results in corresponding levels of lysozyme activity. Further study on the interaction of sulfated chitosans with lysozyme by surface plasmon resonance （SPR） suggested that their affinities might be determined by their molecular structures.

关 键 词：LYSOZYME Sulfated chitosan Activity Structure Regioselective modification. 

分 类 号：O636.1[理学—高分子化学]