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JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) . Vol. XCVIII, N° 11Mention de date : 11/2003Paru le : 15/11/2003 |
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Ajouter le résultat dans votre panierNew advances in tannery logistics and automation / Walter Hottinger in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVIII, N° 11 (11/2003)
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Titre : New advances in tannery logistics and automation Type de document : texte imprimé Auteurs : Walter Hottinger, Auteur Année de publication : 2003 Article en page(s) : p. 425-430 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage En ligne : https://drive.google.com/file/d/1bfYWvfLpk3n9Bt1D-8MAAkT0kM_o6gBH/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4164
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Code-barres Cote Support Localisation Section Disponibilité 001593 - Périodique Bibliothèque principale Documentaires Disponible Polymer binders manufacturing processes and properties with particular consideration of NMP - problems / Wolfang Wenzel in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVIII, N° 11 (11/2003)
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Titre : Polymer binders manufacturing processes and properties with particular consideration of NMP - problems Type de document : texte imprimé Auteurs : Wolfang Wenzel, Auteur Année de publication : 2003 Article en page(s) : p. 431-434 Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure En ligne : https://drive.google.com/file/d/1rxc5GEWfTYpYDYHl3SNqedmH18i5BVOn/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4165
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Code-barres Cote Support Localisation Section Disponibilité 001593 - Périodique Bibliothèque principale Documentaires Disponible Enzymatic modification of hydrolysis products from collagen using a microbial transglutaminase. III. Preparation of films with improved mechanical properties / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVIII, N° 11 (11/2003)
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Titre : Enzymatic modification of hydrolysis products from collagen using a microbial transglutaminase. III. Preparation of films with improved mechanical properties Type de document : texte imprimé Auteurs : Maryann M. Taylor, Auteur ; Eleanor M. Brown, Auteur ; William N. Marmer, Auteur ; Cheng-Kung Liu, Auteur Année de publication : 2003 Article en page(s) : p. 435-444 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Previous work from this laboratory demonstrated that films prepared from gelatins that had been enzymatically modified with microbial transglutaminase had improved tensile strength and toughness, were less soluble in water than gelatin alone and had improved hydrophilic properties. In the present study, our goal was to further enhance functional properties of the enzymatically prepared films and at the same time determine if biodegradability is retained. Orienting films has been described as a method to improve mechanical properties. We found that tensile strength, maximum strain, and Young's Modulus improved significantly when orientation took place on either unmodified or crosslinked dry gelatin films or on films that were swollen in water and then were subsequently dried in the strained position. We further demonstrated that the temperature of drying affects mechanical properties; drying at ambient temperature gives products with significantly higher tensile strength and reduced maximum strain over those products that had been dried at a higher temperature. Furthermore, we found that mechanical properties of strained and unstrained films, dried at ambient temperature, will give similar tensile strengths, thus indicating the importance of careful drying in film preparation. Finally, when polyvinyl alcohol was added to the gelatin mixture, films with improved tensile strength and maximum strain were obtained. In all studies, not only was biodegradability demonstrated but it was also found that by enzymatically modifying the gelatin, the resulting products were superior. En ligne : https://drive.google.com/file/d/1M2Qt5WzslSGYHiiFn-Ct8QNDW0aCzLgs/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4166
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Code-barres Cote Support Localisation Section Disponibilité 001593 - Périodique Bibliothèque principale Documentaires Disponible Molecular level understanding of tanning using an organo-zirconium complex / Balaraman Madhan in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVIII, N° 11 (11/2003)
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Titre : Molecular level understanding of tanning using an organo-zirconium complex Type de document : texte imprimé Auteurs : Balaraman Madhan, Auteur ; Balachandran Unni Nair, Auteur ; Jonnalagadda Raghava Rao, Auteur ; N. N. Fathima, Auteur Année de publication : 2003 Article en page(s) : p. 445-450 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : Organo-zirconium (Organozir) is a zirconium tanning salt complexed with organic moieties. The development of this tanning salt as a potential substitute for chromium has been reported in our earlier work. In the present investigation, studies to understand the mechanism of tanning using organozir at the molecular level have been attempted. The thermal and enzymatic stability of collagen brought about by organozir have been studied using hydrothermal shrinkage measurement, differential scanning calorimetry (DSC) and hydroxyproline estimation respectively. It has been observed that collagen tanned with organozir exhibits a hydrothermal shrinkage temperature of 94°C. The denaturation peak temperature observed from DSC, which indicates the helix → coil transition of collagen, also occurs at 94°C. Mechanistic insights into the stability of collagen against collagenase have been addressed by studying the conformational changes occurring in collagen as a result of interaction with organozir using circular dichroism (CD). The interaction with organo-zirconium complex results only in minor changes in the triple helical conformation of collagen. This indicates that organozir stabilizes collagen against collagenase degradation by blocking the active site in collagen. En ligne : https://drive.google.com/file/d/1qNz8q9ASgpqGjcyvyJwUrruNK4OctFSe/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4167
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Code-barres Cote Support Localisation Section Disponibilité 001593 - Périodique Bibliothèque principale Documentaires Disponible
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Code-barres | Cote | Support | Localisation | Section | Disponibilité |
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001593 | - | Périodique | Bibliothèque principale | Documentaires | Disponible |