2022
DOI: 10.1016/j.carbpol.2022.119844
|View full text |Cite
|
Sign up to set email alerts
|

Tannic acid post-treatment of enzymatically crosslinked chitosan-alginate hydrogels for biomedical applications

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

3
26
0

Year Published

2022
2022
2024
2024

Publication Types

Select...
10

Relationship

3
7

Authors

Journals

citations
Cited by 51 publications
(29 citation statements)
references
References 79 publications
3
26
0
Order By: Relevance
“…Furthermore, the UV spectra (Fig. 2C) displayed a new peak at 275 nm for Ch-Ph, which aligns with the 1 H NMR results confirming the successful conjugation of propionic acid on the chitosan backbone [88].…”
Section: Synthesis Of Ch-ph and Alg-ty Conjugatessupporting
confidence: 81%
“…Furthermore, the UV spectra (Fig. 2C) displayed a new peak at 275 nm for Ch-Ph, which aligns with the 1 H NMR results confirming the successful conjugation of propionic acid on the chitosan backbone [88].…”
Section: Synthesis Of Ch-ph and Alg-ty Conjugatessupporting
confidence: 81%
“…For example, the free radical polymerization can hardly be performed due to TA's strong free-radical scavenging ability. 235,368 Moreover, crosslinking via oxidation of phenolic groups using enzymatic crosslinking can be hindered in the presence of TA owing to the scavenging activity of TA, as well as inhomogeneity due to the complexation of TA with a wide range of polymers.…”
Section: Ta-based Hydrogelsmentioning
confidence: 99%
“…These limitations generated by crosslinking methods can be overcome by using enzymes to form covalently crosslinked hydrogels. Enzyme-mediated crosslinking by tyrosinases [ 16 ], transferases [ 17 ] or peroxidases [ 18 ] have proven their efficiency and therefore, they have attracted increasing attention for application in polymer hydrogel synthesis due to the environmentally-friendly process and the possibility of obtaining biomaterials with extracellular matrix-mimicking properties. Transglutaminase (TGase), a widely present enzyme in nature, has been demonstrated to catalyze the formation of isopeptide bonds between proteins by mimicking in vivo biosynthetic processes, which can significantly improve protein gelation [ 19 , 20 ].…”
Section: Introductionmentioning
confidence: 99%