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Vigorous proteolysis : reliming in the presence of an alkaline protease and bating (post-liming) with an extremophile protease / S. M. Mozersky in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 4 (04/2002)
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Titre : Vigorous proteolysis : reliming in the presence of an alkaline protease and bating (post-liming) with an extremophile protease Type de document : texte imprimé Auteurs : S. M. Mozersky, Auteur ; William N. Marmer, Auteur ; O. Dale Allen, Auteur Année de publication : 2002 Article en page(s) : p. 150-155 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : As part of an investigation into the feasibility of removing from a hide some or all of its decorin while it is being processed into leather, we studied the effects on the physical characteristics of the leather of subjecting the hide to vigorous proteolysis. We used two proteolytic enzyme preparations, one during reliming, and the second for bating post liming. The first is a commercially produced alkaline protease (AP). Extending the work of Alexander in England and of Kronick at Eastern Regional Research Center, ARS, USDA, we found that, for each observed physical property, viz., tensile strength (Smax), Young's modulus (Y), and extensibility (E), the value for the AP-treated samples differed from the corresponding control value by < 6-8% (the least significant difference), thus demonstrating that AP does not adversely affect any of the three physical characteristics. The AP-treated hides are, however, substantially softer and more flexible than the controls. The second protease preparation is one that we made from a halophile selected because it does not produce collagenase. This protease is active in 4M NaCl at a mildly alkaline pH. Bating with the halophile protease in 4M NaCl was found to yield a leather with satisfactory physical characteristics (Smax, Y, and E). High salt concentration will be used experimentally to loosen the tight (albeit non-covalent) bonding of decorin to collagen, thus rendering the proteoglycan more susceptible to proteolysis and removal from the hide. En ligne : https://drive.google.com/file/d/1FkL6j13napjNATdHgURko2lna7B0vxEl/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4313
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCVII, N° 4 (04/2002) . - p. 150-155[article]Réservation
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