文献类型：期刊文献

英文题名：Enhancement of Enzymatic Activity by Magnetic Spherical Polyelectrolyte Brushes: A Potential Recycling Strategy for Enzymes

作者：Xu, Yisheng[1,2];Wang, Siyi[1,3];Han, Haoya[1];Chen, Kaimin[1,4];Qin, Li[1];Xu, Jun[1];Wang, Jie[1];Li, Li[1];Guo, Xuhong[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Chem Engn, Shanghai 200237, Peoples R China;[2]Zhejiang Univ Sci & Technol, Zhejiang Prov Key Lab Chem & Biochem Proc Technol, Sch Biol & Chem Engn, Hangzhou 310023, Zhejiang, Peoples R China;[3]Shanghai Res Inst Chem Ind, Testing Ctr, Shanghai 200062, Peoples R China;[4]Shanghai Univ Engn Sci, Coll Chem & Chem Engn, Shanghai 201620, Peoples R China

年份：2014

卷号：30

期号：37

起止页码：11156

外文期刊名：LANGMUIR

收录：;EI(收录号：20151800806224);WOS:【SCI-EXPANDED(收录号:WOS:000342184600022)】；

基金：Financial support from the National Natural Science Foundation of China (No. 51273063, 11076002/A06, and 21306049), the Fundamental Research Funds for the Central Universities, the higher school specialized research fund for the doctoral program (20110074110003 and 222201314029), and the China Postdoctoral Science Foundation (12Z102060005) is gratefully acknowledged.

语种：英文

外文关键词：Binding energy - Catalyst activity - Recycling - Catalysis - Polyelectrolytes - Titration

摘要：Interactions between amyloglucosidase and magnetic spherical polyelectrolyte brushes (MSPB) were studied by turbidimetric titration, which reveals reversible and tunable behaviors of pH-dependent enzyme-SPB binding. Quantitative thermodyanmic parameters including binding affinity and stoichiometry between enzyme and SPBs were further measured by isothermal titration calorimetry (ITC). A large amount of enzyme can be loaded in MSPB without loss of MSPB stability. We demonstrated that the enzymatic activity of amyloglucosidase bound in MSPB could be greatly enhanced (catalytic reaction rate, k(bound) = 1.361k(free)) compared to free enzyme acitivity in solution. This is tremendous improvement from other carrier systems that usually lead to a significant decrease of enzymatic activity. Both the high enzyme loading capacity and the enhancement of the catalytic activity probably arise from the Coulombic interactions between the enzyme and MSPB. These findings provide a practical strategy for enhancement of enzyme activity and enzyme recycling by MSPB.