Accueil
Détail de l'auteur
Auteur H. E. C. Koon |
Documents disponibles écrits par cet auteur
Ajouter le résultat dans votre panier Affiner la recherche
Link lock : an explanation of the chemical stabilisation of collagen / Anthony D. Covington in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 92, N° 1 (01-02/2008)
[article]
Titre : Link lock : an explanation of the chemical stabilisation of collagen Type de document : texte imprimé Auteurs : Anthony D. Covington, Auteur ; L. Song, Auteur ; Ono Suparno, Auteur ; H. E. C. Koon, Auteur ; M. J. Collins, Auteur Année de publication : 2008 Article en page(s) : p. 1-7 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène -- Analyse
Cuirs et peaux
Dénaturation (chimie)
Oxazolidine
Polyphénols
Réticulation (polymérisation)
Stabilité chimiqueIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Chemical modifications of collagen, of the type known in the leather tanning industry, can raise the denaturation temperature, from 60°C in its natural state, up to 130°C. There are only a few chemical reactions known to be capable of achieving the highest values and these have long been assumed to be unrelated. Here, we show for the first time that all the stabilising mechanisms are fundamentally the same, regardless of chemical type. Any single component of a stabilising reaction has the effect of linking part of the collagen structure into the surrounding matrix of water: the outcome is always to confer moderate hydrothermal stability, up to 85°C. The effect is merely to hinder the shrinking/denaturation transition, so no single component reaction can exceed this moderate result. However, in addition, a second reaction component can be applied in the process, which may have the ability to lock the linked structure together, creating a macromolecular structure around the triple helices. The effect of the concerted interaction with collagen is to prevent more effectively the unravelling of the triple helices and thereby to raise the hydrothermal stability to much higher values of denaturation temperature. This new proposed 'linklock' mechanism opens up the possibility of achieving high collagen stability in new ways, which will contribute to the development of new collagenic biomaterials. Note de contenu : - Table 1 : Typically observed effects on collagen denaturation temperature ranges of some chemical modifications
- Table 2 : The effects of crosslinking polyphenol with oxazolidine on the denaturation temperature, the synergy of the reaction and the effect on the hydrothermal stability of acetone washing to break hydrogen bonding (ΔTs)(°C)
- Table 3 : Relative rates of increase in tension after shrinking transition is initiated and relative rates of decrease in tension after the shrinking transition
- Table 4 : The stabilisation of collagen (as hide powder) by the combination of dihydroxy naphthalene and oxazolidineEn ligne : https://drive.google.com/file/d/1tiLCy85-VTxKSKpatCI-dBw-eoztRNiV/view?usp=share [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=38914
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 92, N° 1 (01-02/2008) . - p. 1-7[article]