Fabrication and characterization of epoxylated zwitterionic copolymergrafted silica nanoparticle as a new support for lipase immobilization

Ning Chen; Chunyu Zhang; Xiaoyan Dong; Yan Sun

Your Location：

Home >

Browse articles >

Fabrication and characterization of epoxylated zwitterionic copolymergrafted silica nanoparticle as a new support for lipase immobilization

Biotechnology and Bioengineering | Updated：2026-01-06

- Fabrication and characterization of epoxylated zwitterionic copolymergrafted silica nanoparticle as a new support for lipase immobilization
- Chinese Journal of Chemical Engineering Vol. 28, Issue 4, Pages: 1129-1135(2020)
- Affiliations：
  
  Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University,Tianjin,China,300354
- Author bio：
- Funds：
- DOI：
  CLC：
- Published：2020
- Accepted：
Scan QR Code
Ning Chen, Chunyu Zhang, Xiaoyan Dong, Yan Sun. Fabrication and characterization of epoxylated zwitterionic copolymergrafted silica nanoparticle as a new support for lipase immobilization[J]. Chinese Journal of Chemical Engineering, 2020, 28(4): 1129-1135.
DOI：

Ning Chen, Chunyu Zhang, Xiaoyan Dong, Yan Sun. Fabrication and characterization of epoxylated zwitterionic copolymergrafted silica nanoparticle as a new support for lipase immobilization[J]. Chinese Journal of Chemical Engineering, 2020, 28(4): 1129-1135. DOI：

摘要

Abstract

Our previous work proved that the thermal stability of

Candida rugosa

lipase (CRL) immobilized on zwitterionic polymer (poly(carboxybetaine methacrylate)) grafted silica nanoparticle (SNP) was much higher than that on poly(glycidyl methecrylate) (pGMA) grafted SNP

while the latter showed significantly increased activity. Inspired by the research

we have herein proposed to synthesize copolymers of zwitterionic sulfobetaine methacrylate (SBMA) and GMA for CRL immobilization. The copolymers were grafted onto SNP surface at three GMA/ SBMA (G/S) molar ratios (G100/S0

G50/S50

G10/S90)

followed by the covalent coupling of CRL to the surface copolymers. The immobilized CRLs on the corresponding supports were denoted as p(G100-S0)-CRL

p(G50-S50)-CRL and p(G10-S90)-CRL. The enzyme loading increased with the increase of GMA content in the copolymer

while the activity varied with the grafted copolymer composition. Kinetic study proved the improvement of enzyme-substrate affinity after immobilization. In comparison to p(G100-S0)-CRL

p(G50-S50)-CRL and p (G10-S90)-CRL presented remarkably enhanced thermal stability and pH tolerance

and p(G10-S90)-CRL

showed the highest stability. These results suggest that the copolymer design is promising for development as a versatile platform for enzyme immobilization.

关键词

Keywords

references

Views

128

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Conjugation of a zwitterionic polymer with dimethyl chains to lipase significantly increases the enzyme activity and stability

Zwitterionic polymer-coated porous poly(vinyl acetate-divinyl benzene) microsphere: A new support for enhanced performance of immobilized lipase

Optimized anchor and cell wall engineering boost UDP-glycosyltransferase display for glycyrrhetinic acid glycosylation in Komagataella phaffii

Immobilization strategies, supporting materials, and performance advantages of photocatalysts in ammonia synthesis

Lipase and photodecarboxylase coexpression: A potential strategy for alkane-based biodiesel production from natural triglycerides

Related Author

Chunyu Zhang

Yan Sun

Xiaoyan Dong

Yifeng Li

Li Chun

Liu Hu

Feng Xudong

Wang Jing

Related Institution

Department of Biochemical Engineering, School of Chemical Engineering and Technology and Key Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Tianjin University

College of Life Sciences, Yantai University

Center for Synthetic & Systems Biology, Tsinghua University

Key Laboratory of Medical Molecule Science and Pharmaceutics Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology

Key Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University

⁰