Issue 2, 2015

Facile immobilization of enzyme on three dimensionally ordered macroporous silica via a biomimetic coating

Abstract

This study describes a general strategy using norepinephrine (NE) as a stable anchor for the immobilization of enzyme onto three-dimensionally ordered macroporous (3DOM) silica. Penicillin G acylase (PGA) was chosen as a model enzyme. The effect of pH and temperature on the activity of PGA@PN–SiO2 (PGA immobilized on poly(norepinephrine)-modified 3DOM silica) was investigated. The operational stability, storage stability and kinetic properties of the PGA@PN–SiO2 were also examined. Compared with free PGA and PGA@SiO2 (PGA immobilized on blank 3DOM silica through physical adsorption), the stabilities of PGA@PN–SiO2 were improved significantly. PGA@PN–SiO2 retained high activity during the hydrolysis in a continuous packed-bed reactor (PBR) after 30 catalytic cycles, which demonstrated that PGA@PN–SiO2 can bear endurance of continuous catalysis. The method presented in this study has broad potential for immobilizing enzymes and other biomolecules.

Graphical abstract: Facile immobilization of enzyme on three dimensionally ordered macroporous silica via a biomimetic coating

Supplementary files

Article information

Article type
Paper
Submitted
03 Nov 2014
Accepted
13 Nov 2014
First published
13 Nov 2014

New J. Chem., 2015,39, 978-984

Facile immobilization of enzyme on three dimensionally ordered macroporous silica via a biomimetic coating

Y. Jiang, Y. Wang, H. Wang, L. Zhou, J. Gao, Y. Zhang, X. Zhang, X. Wang and J. Li, New J. Chem., 2015, 39, 978 DOI: 10.1039/C4NJ01947D

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