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A new method to immobilize urease in silk fibroin membrane by unidirectional nanopore dehydration.
- Source :
-
Biotechnology progress [Biotechnol Prog] 2024 Sep 05, pp. e3502. Date of Electronic Publication: 2024 Sep 05. - Publication Year :
- 2024
- Publisher :
- Ahead of Print
-
Abstract
- The immobilization of free enzymes is crucial for enhancing their stability in different environments, enabling reusability, and expanding their applications. However, the development of a straightforward immobilization method that offers stability, high efficiency, biocompatibility, and modifiability remains a significant challenge. Silk fibroin (SF) is a good carrier for immobilized enzymes and drugs. Here, we employed urease as a model enzyme and utilized our developed technology called unidirectional nanopore dehydration (UND) to efficiently dehydrate a regenerated SF solution containing urease in a single step, resulting in the preparation of a highly functionalized SF membrane immobilizing urease (UI-SFM). The preparation process of UI-SFM is based on an all-water system, which is mild, green and able to efficiently and stably immobilize urease in the membranes, maintaining 92.7% and 82.8% relative enzyme activity after 30 days of storage in dry and hydrated states, respectively. Additionally, we performed additional post-treatments, including stretching and cross-linking with polyethylene glycol diglycidyl ether (PEGDE), to obtain two more robust immobilized urease membranes (UI-SFMs and UI-SFMc). The thermal and storage stability of these two membranes were significantly improved, and the recovery ratio of enzyme activity reached more than 90%. After 10 repetitions of the enzymatic reaction, the activity recovery of UI-SFMs and UI-SFMc remained at 92% and 88%, respectively. The results suggest that both UND-based and post-treatment-developed membranes exhibit excellent urease immobilization capabilities. Furthermore, the enzyme immobilization method offers a straightforward and versatile approach for efficient and stable enzyme immobilization, while its flexible modifiability caters to diverse application requirements.<br /> (© 2024 American Institute of Chemical Engineers.)
Details
- Language :
- English
- ISSN :
- 1520-6033
- Database :
- MEDLINE
- Journal :
- Biotechnology progress
- Publication Type :
- Academic Journal
- Accession number :
- 39238226
- Full Text :
- https://doi.org/10.1002/btpr.3502