Transglutaminase-Catalyzed Bottom-Up Synthesis of Polymer Hydrogel
Enzyme catalysis has attracted increasing attention for application in the synthesis of polymer hydrogel due to the eco-friendly process and the devisable catalytic reaction. Moreover, bottom-up approaches combining enzyme catalysts and molecular self-assembly have been explored for synthesizing hyd...
Saved in:
Published in | Frontiers in bioengineering and biotechnology Vol. 10; p. 824747 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Frontiers Media S.A
22.03.2022
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Enzyme catalysis has attracted increasing attention for application in the synthesis of polymer hydrogel due to the eco-friendly process and the devisable catalytic reaction. Moreover, bottom-up approaches combining enzyme catalysts and molecular self-assembly have been explored for synthesizing hydrogel with complex architectures. An enzyme widely distributed in nature, transglutaminase (TGase) has been confirmed to catalyze the formation of isopeptide bonds between proteins, which can effectively improve the gelation of proteins. In this mini-review, TGase-catalyzed synthesis of polymer hydrogels, including fibrin hydrogels, polyethylene glycol hydrogels, soy protein hydrogels, collagen hydrogels, gelatin hydrogels and hyaluronan hydrogels, has been reviewed in detail. The catalytic process and gel formation mechanism by TGase have also been considered. Furthermore, future perspectives and challenges in the preparation of polymer hydrogels by TGase are also highlighted. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 Reviewed by: Ashley Carson Brown, North Carolina State University, United States This article was submitted to Bioprocess Engineering, a section of the journal Frontiers in Bioengineering and Biotechnology Edited by: Jennifer Ann Littlechild, University of Exeter, United Kingdom |
ISSN: | 2296-4185 2296-4185 |
DOI: | 10.3389/fbioe.2022.824747 |