| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 4752852 | Enzyme and Microbial Technology | 2017 | 5 Pages |
â¢Protein-based inverse opals were prepared for the first time.â¢The properties of the immobilized PGA were investigated.â¢The immobilized PGA showed improved thermal and pH stability.â¢The immobilized PGA can be applied in continuous catalysis in packed-bed reactor.
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.
Graphical abstractA facile approach was provided to prepare protein-based inverse opals for the first time and the obtained opals were used to immobilize enzyme.Download high-res image (162KB)Download full-size image
