Content:
Fish collagen has been considered to be an alternative for mammalian collagen, however, physicochemical properties of fish collagen-based materials such as gels are so far not adequate for actual application. In the present study, we prepared two types of fish collagen gels with sufficient elasticity: i) dehydrated fibrillogenesis collagen gels (DFCG), which were fabricated via collagen self-assembly followed by immersion in different concentrations of ethanol solutions, and ii) dehydrated cross-linking collagen gels (DCCG), which were fabricated via collagen self-assembly and simultaneous cross-linking followed by immersion in ethanol solution. Furthermore, the physicochemical properties of DFCG and DCCG were analyzed by atomic force microscopy, differential scanning calorimetry, enzymatic degradation and dynamic viscoelastic measurements. The microstructure of DFCG was consisted of characteristic Dperiodic collagen fibrils and insusceptible of ethanol concentrations (20-100% (v/v)). However, the thermal
stability, remaining weight after enzymatic degradation and mechanical properties of DFCG distinctly increased with the increase of ethanol dose, possiblely ascribing that ethanol with higher polarity might
dehydrate partial free water of DFCG and strengthen the interactions of hydrogen bond. Especially, for the gel treated by 100% (v/v) enthanol, Td increased by 32.7 °C and G′ was 55-folds than those of
undehydrated gel (43.1 °C and 239.2 Pa). In the case of DCCG, the formation of collagen fibrils was depended on the concentrations of N-hydroxysuccinimide adipic acid derivative (NHS-AA), which was
converted to [NHS-AA]/[NH2] ratios (calculated by the [active ester group] of NHS-AA and [ε-NH2] of lysine and hydroxylysine residues of collagen). As the ratio= 0.05, the characteristic D-periodic fibrils were still formed and the treatment of 60% (v/v) ethanol increased the Td (52.5 °C) and G′ (7388 Pa) values of the gel compared with those of uncross-linked gel (49 °C and 2064.32 Pa, respectively), majorly resulting from the effects of covalent cross-linking bonds and hydrogen bonds. However, when the ratio= 0.2, the collagen self-assembly was intensively inhibited and the dehydration of free water within gel structure in the absence of thick fibrils led to the shrinkage of the gel and an obvious decrease in Td (42 °C) and G′ (432 Pa). Although the [NHS-AA]/[NH2] ratio further increased to 0.8, the thermal stability and elasticity of the gel enhanced mildly suggesting that the presence of thick fibrils formed via the self-assembly was significantly crucial for reinforcing the gels.
Take-Away:
The fish collagen gels with excellent elasticity were prepared via the treatment of ethanol.
The physicochemical properties of the dehydrated gels were depended on the concentrations of ethanol.
The presence of characteristic D-periodic fibrils was significantly crucial for reinforcing the gels.
| Identifer | oai:union.ndltd.org:DRESDEN/oai:qucosa:de:qucosa:34167 |
| Date | 26 June 2019 |
| Creators | Shen, Lirui, Xu, Songcheng, Wu, Kun, Li, Guoying |
| Contributors | International Union of Leather Technologists and Chemists Societies |
| Publisher | Verein für Gerberei-Chemie und -Technik e. V., Forschungsinstitut für Leder und Kunststoffbahnen (FILK) gGmbH |
| Source Sets | Hochschulschriftenserver (HSSS) der SLUB Dresden |
| Language | English |
| Detected Language | English |
| Type | info:eu-repo/semantics/publishedVersion, doc-type:conferenceObject, info:eu-repo/semantics/conferenceObject, doc-type:Text |
| Rights | info:eu-repo/semantics/openAccess |
| Relation | urn:nbn:de:bsz:14-qucosa2-340872, qucosa:34087 |
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