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

被引:35
|
作者
Jiang, Yanjun [1 ]
Wang, Yaping [1 ]
Wang, Hua [1 ]
Zhou, Liya [1 ]
Gao, Jing [1 ]
Zhang, Yufei [2 ]
Zhang, Xu [1 ]
Wang, Xiaomei [1 ]
Li, Jian [3 ]
机构
[1] Hebei Univ Technol, Sch Chem Engn & Technol, Tianjin 300130, Peoples R China
[2] Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
[3] Tianjin Univ Sci & Technolgy, Coll Mat Sci & Chem Engn, Tianjin 300457, Peoples R China
关键词
PENICILLIN-G ACYLASE; MESOSTRUCTURED CELLULAR FOAMS; MESOPOROUS SILICA; CROSS-LINKING; BIOCATALYSTS; IMPROVEMENT; STABILITY; LIPASE;
D O I
10.1039/c4nj01947d
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:978 / 984
页数:7
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