Role of chlorogenic acid and procyanidin in the modification of self-assembled fibrillar gel prepared from tilapia collagen. (December 2022)
- Record Type:
- Journal Article
- Title:
- Role of chlorogenic acid and procyanidin in the modification of self-assembled fibrillar gel prepared from tilapia collagen. (December 2022)
- Main Title:
- Role of chlorogenic acid and procyanidin in the modification of self-assembled fibrillar gel prepared from tilapia collagen
- Authors:
- An, Xiangsheng
Duan, Shujun
Jiang, Zhicong
Chen, Sunan
Sun, Wenxuan
Liu, Xiaoyan
Sun, Zhonghao
Li, Yinping
Yan, Mingyan - Abstract:
- Highlights: The equilibrium cross-linking degree was much higher with PC than CGA. There were primarily hydrogen bonding interactions between polyphenols and CFG. PC improved water absorption and retention capacity of gel. Mechanical properties and enzymatic resistance of gel were improved by PC. Gels showed good antioxidant and antibacterial capacity. Abstract: Collagen fibrillar gels (CFG), formed by self-assembly, displayed similar structure and properties to native tissues. Plant polyphenols showed antioxidant and antibacterial capacity, etc. Previous reports stated introduction of polyphenols could improve the properties of collagen-based material. However, only a few studies were reported on the modification of CFG by polyphenols. In the study, tilapia CFG was cross-linked with chlorogenic acid (CGA) and procyanidin (PC), respectively. The cross-linking conditions were investigated. Results showed PC endowed CFG with higher cross-linking effect at saturation than CGA. ATR-FTIR and XPS displayed there were stronger hydrogen bonds between -OH groups of PC and C = O groups of CFG, but weaker in CGA, confirmed by molecular docking simulation. XRD and SEM indicated PC induced the denser network formed by thinner fibrils, not present in CGA. As a result, water absorption and retention capacity, mechanical properties and enzymatic resistance of gel were improved evidently, whereas thermal stability reduced. Additionally, polyphenol cross-linking granted better antioxidantHighlights: The equilibrium cross-linking degree was much higher with PC than CGA. There were primarily hydrogen bonding interactions between polyphenols and CFG. PC improved water absorption and retention capacity of gel. Mechanical properties and enzymatic resistance of gel were improved by PC. Gels showed good antioxidant and antibacterial capacity. Abstract: Collagen fibrillar gels (CFG), formed by self-assembly, displayed similar structure and properties to native tissues. Plant polyphenols showed antioxidant and antibacterial capacity, etc. Previous reports stated introduction of polyphenols could improve the properties of collagen-based material. However, only a few studies were reported on the modification of CFG by polyphenols. In the study, tilapia CFG was cross-linked with chlorogenic acid (CGA) and procyanidin (PC), respectively. The cross-linking conditions were investigated. Results showed PC endowed CFG with higher cross-linking effect at saturation than CGA. ATR-FTIR and XPS displayed there were stronger hydrogen bonds between -OH groups of PC and C = O groups of CFG, but weaker in CGA, confirmed by molecular docking simulation. XRD and SEM indicated PC induced the denser network formed by thinner fibrils, not present in CGA. As a result, water absorption and retention capacity, mechanical properties and enzymatic resistance of gel were improved evidently, whereas thermal stability reduced. Additionally, polyphenol cross-linking granted better antioxidant activity to gel, PC resulting in higher DPPH and PTIO radical scavenging ratio, while CGA showing higher Fe(II) chelation ratio. It also induced better antibacterial activity against Staphylococcus aureus, especially PC cross-linking. The results revealed CFG cross-linked by PC showed better properties compared with CGA, making it have potential application in biomaterials. … (more)
- Is Part Of:
- Polymer degradation and stability. Volume 206(2022)
- Journal:
- Polymer degradation and stability
- Issue:
- Volume 206(2022)
- Issue Display:
- Volume 206, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 206
- Issue:
- 2022
- Issue Sort Value:
- 2022-0206-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-12
- Subjects:
- Collagen -- Cross-linking -- Chlorogenic acid -- Procyanidin -- Gel
Polymers -- Deterioration -- Periodicals
Stabilizing agents -- Periodicals
Polymères -- Dégradation -- Périodiques
Stabilisants -- Périodiques
668.9 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01413910 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.polymdegradstab.2022.110177 ↗
- Languages:
- English
- ISSNs:
- 0141-3910
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6547.704700
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 24456.xml