| Titre : |
Effects of pretanning processes on bovine hide collagen structure |
| Type de document : |
texte imprimé |
| Auteurs : |
Eleanor M. Brown, Auteur ; Renée J. Latona, Auteur ; Maryann M. Taylor, Auteur ; Rafael A. Garcia, Auteur |
| Année de publication : |
2012 |
| Article en page(s) : |
p. 1-7 |
| Note générale : |
Bibliogr. |
| Langues : |
Américain (ame) |
| Catégories : |
Collagénases Les collagénases sont des enzymes capables de rompre les liaisons peptidiques du collagène. Elles facilitent la destruction des structures extracellulaires lors de la pathogenèse bactérienne. Ce sont des exotoxines.
La production de collagénases peut être induite lors d'une réponse immunitaire, par les cytokines qui stimulent les cellules telles que les fibroblastes et les ostéoplastes et occasionnent indirectement des lésions tissulaires.
Collagène
Cuirs et peaux
Electrophorèse
Microscopie électronique à balayage
Prétannage
Stabilité thermique
|
| Index. décimale : |
675.2 Préparation du cuir naturel. Tannage |
| Résumé : |
The US meat industry currently produces approximately 35 million cattle hides annually as its most valuable coproduct. These hides serve as raw material, first for the leather industry, and then for the gelatin, and biomaterials industries. The conversion of animal hides into leather is a multistep process that has evolved more as art form than as science. Economic or environmental issues typically dictate changes in beam-house processes that prepare the hide for tanning. The tanner evaluates these changes, in terms of impact on tannery costs and quality of leather produced. Thus far, the effects of beam-house processes on the molecular characteristics of collagen have received little attention. The basis for tanning and most biomaterials applications is the stabilization of the collagen matrix, thus any changes to the molecular characteristics of hide collagen may be expected to impact these applications. This study showed that while the effects of different dehairing processes on the structure and stability of monomeric collagen were similar, the effects on the collagen fiber structure were distinct. These results are anticipated to assist the tanner as well as the manufacturers of collagen-based biomaterials and gelatin to better understand their substrate and changes to it that may occur when beam-house processes are altered. |
| Note de contenu : |
- Materials
- Sample preparation : powdered hide - Extracted collagen
- Analyses - Scanning Electron Microscopy (SEM) - Susceptibility to collagenase - Electrophoresis - Hydrothermal stability of powdered hide - Thermal stability of extracted collagen
- RESULTS AND DISCUSSION : Scanning Electron Microscopy (SEM) - Susceptibility to collagenase - Hydrothermal stability of powdered hide - Thermal stability of extracted collagen |
| En ligne : |
https://drive.google.com/file/d/1HTNem7IR_uqd6Jser9U60Bz_eD4ySqLG/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=13296 |
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CVII, N° 1 (01/2012) . - p. 1-7
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