文献类型：期刊文献

英文题名：Esterase-Immobilized Sea-Urchin-Like Fe3O4 Nanoparticles for Chloramphenicol Palmitate Synthesis

作者：Dong, Fengying[1,2];Lin, Lin[3];Su, Yue[2];Zhang, Chuan[2];Wei, Wei[1]

机构：[1]East China Univ Sci & Technol, Newworld Inst Biotechnol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China;[2]Shanghai Jiao Tong Univ, Frontiers Sci Ctr Transformat Mol, Sch Chem & Chem Engn, State Key Lab Met Matrix Composites, 800 Dongchuan Rd, Shanghai 200240, Peoples R China;[3]Shanghai Inst Technol, Sch Chem & Environm Engn, Shanghai 201418, Peoples R China

年份：2023

卷号：153

期号：7

起止页码：1974

外文期刊名：CATALYSIS LETTERS

收录：;EI(收录号：20223512667739);WOS:【SCI-EXPANDED(收录号:WOS:000847049300001)】；

基金：This research was financially supported by the National Natural Science Foundation of China (Grant No. C31570795), the Shanghai outstanding technical leaders plan 19XD1431800, the National Natural Science Foundation of China (Grant Nos. 81830052 and 81530053) and Shanghai Key Laboratory of Molecular Imaging (Grant No. 18DZ2260400).

语种：英文

外文关键词：Polydopamine-coated Fe3O4 nanoparticle; Dialdehyde starch; Esterase; Compartmentation immobilization; Regio-selectivity; Chloramphenicol palmitate

摘要：Mostly, enzyme activity is greatly reduced after immobilization due to unfavourable conformational change occurred during the immobilization procedure. Herein, we report a novel magnetic nanoparticle-based platform for Bacillus altitudinis esterase (EstBASASP) immobilization using dialdehyde starch (DAS) as a molecular glue. First polydopamine (PDA) was coated on the surface of Fe3O4 nanoparticles (Fe3O4 NPs) with a controllable thickness. Thereafter, PDA-functionalized Fe3O4 NPs were modified with dialdehyde starch (DAS) to provide the aldehyde groups, which was employed as a glue to further fix the EstBASASP on particle surface via covalent bonding, resulting in the formation of a sea-urchin-like esterase-immobilized magnetic nanoparticle. The obtained nanoparticles (Fe3O4@PDA/DAS) achieved an enzyme load of 162.72 mg/g and retained 65.7% of its specific enzyme activity, demonstrating better thermal and storage stability compared with the "polydopamine-coated" nanoparticles (Fe3O4@PDA) and free EstBASASP. In addition, in a chloramphenicol palmitate synthesis, the immobilized esterase (EstBASASP-Fe3O4@PDA/DAS) gave 99% conversion and purity in 21 h (chloramphenicol: 0.15 M, enzyme dosage: 50 mg/mL) and retained over 80% of its activity after 12 cycles. This study provides a general strategy for immobilizing enzyme on nanoparticles and employs them as a novel platform for enzyme-mediated biocatalytic reaction. [GRAPHICS] .