Remarkably enhanced activity and substrate affinity of lipase covalently bonded on zwitterionic polymer-grafted silica nanoparticles

Journal of Colloid and Interface Science
Chunyu ZhangYan Sun

Abstract

Enzymes are promising biocatalysts for the production or degradation of chemical compounds, but low stabilities of free enzymes restrict their industrial applications. Therefore, development of effective immobilization methods to maintain or increase enzyme activity and stability remains a challenge. In this work, a novel support made of zwitterionic polymer-grafted silica nanoparticles (p-SNPs) was fabricated and Candida rugosa lipase (CRL) was covalently attached onto the p-SNPs. The zwitterionic polymer was a product of the reaction between poly(maleic anhydride-alt-1-octadecene) and N,N-dimethylenediamine and contained a cetane side chain. The hydrolytic activity, reaction kinetics, thermal stability, pH tolerance, storage stability and reusability of the immobilized CRL (SNPs-CRL) were investigated. It revealed that the specific activity of SNPs-CRL was two to four times higher than the free CRL in the temperature range of 25-60 °C. It is considered mainly due to the interfacial activation effect regulated by the cetane side chains of the zwitterionic polymer. Kinetic studies revealed remarkable improvement of the enzymatic reaction efficiency by the immobilized enzyme as demonstrated by the significant increases of the re...Continue Reading

Citations

Nov 18, 2018·Soft Matter·Qingyi XieGuangzhao Zhang
Mar 29, 2020·Chemical Communications : Chem Comm·Hui LiWeimin Tan
Aug 28, 2020·Frontiers in Bioengineering and Biotechnology·Andoni Rodriguez-AbetxukoAna Beloqui
Jul 6, 2021·Colloids and Surfaces. B, Biointerfaces·Hongbo SuoLili Xu
Jul 24, 2021·International Journal of Biological Macromolecules·Abdallah R IsmailKwang-Hyun Baek

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