文献类型：期刊文献

英文题名：Low-cost mussel inspired poly(Catechol/Polyamine) modified magnetic nanoparticles as a versatile platform for enhanced activity of immobilized enzyme

作者：Tang, Wen[1];Chen, Chao[2];Sun, Wen[2];Wang, Ping[2,3];Wei, Dongzhi[1]

机构：[1]East China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Sch Biotechnol, Biomed Nanotechnol Ctr, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[3]Univ Minnesota, Dept Bioprod & Biosyst Engn, St Paul, MN 55108 USA

年份：2019

卷号：128

起止页码：814

外文期刊名：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

收录：;EI(收录号：20242616372919);WOS:【SCI-EXPANDED(收录号:WOS:000463305100094)】；

基金：This work was supported by the National Natural Science Foundation of China (No. 31471659, 21636003 and 21672065) and the Fundamental Research Funds for the Central Universities (No. 22221818014). The authors thank Research Center of Analysis and Test of East China University of Science and Technology for the help on the characterization.

语种：英文

外文关键词：Catechol/Polyamine; Spacer-arm; Magnetic nanoparticles; Lipase; Enzyme immobilization

摘要：Owing to dopamine's excellent adhesion ability and easy modification, it has been widely applied for enzyme immobilization, while the high cost of dopamine and low activity recovery of immobilized enzyme highly impede large-scale application of immobilized enzyme. We herein developed a low-cost and ideal activity recovery enzyme immobilization strategy based on magnetic nanoparticles by replacing dopamine with cheap Catechol/tetraethylene pentamine (CPA) binary system and introducing spacer-arms. In brief, CPA was first polymerized and deposited on the surface of magnetic nanoparticles with a modified mussel-inspired method, and the generated poly(CPA) layer was further functionalized with ethylene glycol diglycidyl ether (EGDE) molecules as spacer-arms for enzyme immobilization. Subsequently, lipases as model enzymes were firmly immobilized on the surface of such amino-epoxy functionalized magnetic materials through ion exchange and covalent attachment with 180.6 mg/g support of loading capacity and 69.2% of activity recovery under the optimized conditions. Furthermore, the immobilized lipase exhibited the improved tolerance rang of pH, temperature and storage stability as well as excellent reusability. Most strikingly, the theoretical simulation and secondary structure analysis of immobilized lipase revealed that the biocompatible microenvironment and flexible tethering at interface could effectively improve performance of the immobilized enzyme and stability. Thus, this novel immobilized enzyme strategy will open up a new perspective for the development of enzyme immobilization and lower the cost of immobilized enzyme in large-scale industrial application. (C) 2019 Elsevier B.V. All rights reserved.