Protein-based inverse opals: A novel support for enzyme immobilization

被引：12

作者：

Jiang, Yanjun ^{[1
]}

Sun, Wenya ^{[1
]}

Wang, Yaping ^{[1
]}

Wang, Lihui ^{[1
]}

Zhou, Liya ^{[1
]}

Gao, Jing ^{[1
,2
]}

He, Ying ^{[1
]}

Ma, Li ^{[1
]}

Zhang, Xu ^{[1
]}

机构：

[1] Hebei Univ Technol, Sch Chem Engn & Technol, Guangrong Rd, Tianjin 300130, Peoples R China

[2] Hebei Univ Technol, Hebei Prov Key Lab Green Chem Technol & High Effi, 8 Guangrong Rd, Tianjin 300130, Peoples R China

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2017年 / 96卷

关键词：

Protein-based inverse opal; Immobilized enzyme; Penicillin G acylase; Biocatalysis; PENICILLIN-G ACYLASE; CONFORMATIONAL-CHANGES; CATALYTIC COMPETENCE; IONIC LIQUIDS; BIOCATALYSIS; SILICA; NANOPARTICLES; MICROSPHERES; STABILITY; FACILE;

D O I：

10.1016/j.enzmictec.2016.08.021

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In this study, protein-based inverse opals were prepared for the first time by using the colloidal crystal templating method. The preparation process involved three steps including filling the templates with protein molecules, crosslinking, and template removal. The obtained inverse opals were used to immobilize Penicillin G acylase (PGA) because of its intrinsic biocompatible property. The immobilization process was optimized and the properties of the immobilized PGA (PGA@IO) were investigated. PGA@IO exhibited improved thermal and pH stability compared with its free counterpart. After reusing nine times, it retained 70% of the initial activity. Besides, the PGA@IO retained high activity during the hydrolysis reactions in continuous catalysis in packed-bed reactor (PBR) after 15 days. (C) 2016 Elsevier Inc. All rights reserved.

引用

页码：42 / 46

页数：5

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