[article]
| Titre : |
A comparison of chemical, physical and enzymatic crosslinking of bovine type I collagen fibrils |
| Type de document : |
texte imprimé |
| Auteurs : |
Andrew Lastowka, Auteur ; Gennaro J. Maffia, Auteur ; Eleanor M. Brown, Auteur |
| Année de publication : |
2005 |
| Article en page(s) : |
p. 196-202 |
| Note générale : |
Bibliogr. |
| Langues : |
Américain (ame) |
| Index. décimale : |
675 Technologie du cuir et de la fourrure |
| Résumé : |
Insoluble type I collagen fibrils are used in several biotechnological research applications including artificial organ scaffolding, skin grafts and cell immobilization beads for fluidized bed reactors. In these applications, collagen is usually strengthened against enzymatic degradation and physical stresses by the addition of cross-links. A suitable collagen source for these purposes appears to be bovine corium, from the lower split of a fleshed hide, a by-product of the leather industry. The present study on ball-milled bovine type I collagen examined the documented cross-linking capabilities of glutaraldehyde and dehydrothermal drying with the relatively new enzymatic cross-linking technique involving microbial transglutaminase. To assess the degree of cross-linking by each technique, free amine residues remaining after cross-linking, collagenase resistance and size of cross-linked complexes were determined. Glutaraldehyde cross-linking resulted in the least number of free amines, highest molecular weight aggregates and highest resistance to collagenase degradation. Dehydrothermal drying also produced high molecular weight aggregates, but partially hydrolyzed the protein, making the fibril more susceptible to collagenase. Microbial transglutaminase treated collagen produced large molecular weight aggregates and was more resistant to collagenase degradation than control collagen. This new cross-linking technique warrants additional research attention. |
| En ligne : |
https://drive.google.com/file/d/1D7vQjt_L_mlKI7riEvxjPUN5GY86B99K/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4067 |
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. C, N° 5 (05/2005) . - p. 196-202
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A comparison of chemical, physical and enzymatic crosslinking of bovine type I collagen fibrils in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. C, N° 5 (05/2005)
