| Titre : |
Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids |
| Type de document : |
texte imprimé |
| Auteurs : |
Sicong Liu, Auteur ; Qian Li, Auteur ; Li Guoying, Auteur |
| Année de publication : |
2019 |
| Article en page(s) : |
12 p. |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Bovins -- Races
Chimie analytique
Collagène
Collagène -- Analyse
Collagène -- Solubilité
Dispersions et suspensions
Liquides ioniques
|
| Index. décimale : |
675 Technologie du cuir et de la fourrure |
| Résumé : |
The dissolution of collagen in ionic liquids (ILs) was highly dependent on the polarity of ILs, which was influenced by their sorts and concentrations. Herein, the solubility and dispersion degree of collagen in two sorts of ILs, namely 1-ethyl-methylimidazolium tetrafluoroborate ([EMIM][BF4]) with low polarity and 1-ethyl-3-methylimidazolium acetate ([EMIM][Ac]) with high polarity in a concentration range from 10% to 70% at 10 °C were investigated. When 150 mg of collagen was added to 30 mg of ILs, the minimum soluble collagen concentration was 0.02 mg/mL in 70% [EMIM][BF4] with lowest polarity and the maximum was 3.57 mg/mL in 70% [EMIM][Ac] with highest polarity, which indicates that soluble collagen and insoluble collagen fibers were both present. For insoluble collagens, differential scanning calorimetry showed that the thermal-stability was weakened when increasing the ILs concentration and polarity, and the fiber arrangement was looser with a more uniform lyophilized structure, observed by atomic force microscopy and scanning electron microscopy. For soluble collagens, electrophoresis patterns and Fourier transform infrared spectroscopy showed that no polypeptide chain degradation occurred during dissolution, but the thermal denaturation temperature decreased by 0.26 °C~ 7.63 °C with the increase of ILs concentrations, measured by ultra-sensitive differential scanning calorimetry. Moreover, the aggregation of collagen molecules was reduced when ILs polarity was increased as determined by fluorescence measurements and dynamic light scattering, which resulted in an increased loose fiber arrangement observed by atomic force microscopy. If the structural integrity of collagen needs to be retained, then the ILs sorts and concentrations should be considered. |
| Note de contenu : |
- EXPERIMENTAL : Materials - Processing collagen with ILs - Collagen solubility in ILs - DSC of insoluble collagen fibrils - SEM of insoluble collagen fibrils - AFM measurements of insoluble and soluble collagen - SDS–PAGE patterns of soluble collagen - FTIR of soluble collagen - Fluorescence measurements of soluble collagen - DLS measurements of soluble collagen
- RESULTS AND DISCUSSION : Solubility of collagen in ILs - Thermal analysis of insoluble collagen fibrils - SEM images of insoluble collagen fibrils - AFM images of insoluble collagen fibrils - SDS-PAGE patterns of soluble collagen - FTIR spectra analysis of soluble collagen - Thermal analysis of soluble collagen - Fluorescence analysis of soluble collagen - DLS analysis of soluble collagen - AFM images of soluble collagen
- Table 1 The concentration of soluble collagen in different ILs and concentrations
- Table 2 Thermodynamic parameters of Col and collagen samples dissolved in different concentrations of [EMIM][Ac]a |
| DOI : |
https://doi.org/10.1186/s42825-019-0013-9 |
| En ligne : |
https://link.springer.com/content/pdf/10.1186/s42825-019-0013-9.pdf |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=36945 |
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 1 (Année 2019) . - 12 p.
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