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675 : Technologie du cuir et de la fourrure |
Ouvrages de la bibliothèque en indexation 675
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Collagen fiber opening of cattle hides in urea/calcium hydroxide solutions / Qian Zhang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVI, N° 5 (05/2021)
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Titre : Collagen fiber opening of cattle hides in urea/calcium hydroxide solutions Type de document : texte imprimé Auteurs : Qian Zhang, Auteur ; Jie Liu, Auteur ; Xiumin Li, Auteur ; Hui Liu, Auteur ; Yadi Hu, Auteur ; Keyong Tang, Auteur Année de publication : 2021 Article en page(s) : p. 147-154 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Chaulage
Chaux
Cuirs et peaux de bovins
Eaux usées -- Analyse
Fibrilles de collagèneLa fibrille de collagène est une structure constituée d'un assemblage de fibres de tropocollagène (assemblage de 3 protéines de collagène alpha (alpha 1 - alpha 1 - alpha 2) en une hélice droite.
Gonflement (physique)
Hydroxyproline
pH
ProtéoglycanesUn protéoglycane est une glycoprotéine, combinaison d'une protéine et d'un glycosaminoglycane (GAG). L'association entre les deux types de chaîne s'effectue essentiellement dans l'appareil de Golgi, mais également au niveau du réticulum endoplasmique d'une cellule. La proportion de glucides des protéoglycanes peut atteindre 95 %. Ceux-ci se présentant sous la forme d'une ou plusieurs chaînes de glycosaminoglycanes non ramifiées. Les chaînes de sucres sont très longues mais pas ramifiées. Ils sont O-glycosylés, se lient à l'acide aminé sérine à l'extrémité OH. Les protéoglycanes peuvent être soit transportés à l'extérieur de la cellule par exocytose (s'intégrant alors à la matrice extracellulaire sous forme de chondroïtine-sulfate, kératan-sulfate, héparan-sulfate, dermatan-sulfate, etc.), soit entrer dans la constitution de la membrane plasmique ou du glycocalyx, jouant alors un rôle dans les relations cellule-matrice.
Les PG (protéoglycanes) ont des compositions et poids moléculaire très variés et sont hétérogènes au niveau de leur structure et de leur fonction.
Les protéoglycanes sont des composants essentiels de la matrice extracellulaire. Ce sont des pièges à eau qui sont importants pour les propriétés mécaniques des tissus cartilagineux par exemple. Les héparan sulfates peuvent avoir un rôle dans la signalisation : ce sont des co-récepteurs pour les FGF (Fibroblast Growth Factor). Les protéoglycanes jouent aussi un rôle dans la diffusion des molécules de signalisation (Wnt, Shh), ou bien en interagissant avec des inhibiteurs (Noggin). (Wikipedia)
Travail de rivière (cuir)
UréeIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : In the beamhouse, liming might directly affect the structure and performance of collagen, as well as the quality of resultant leather. However, the influences of composition and content of liming agents on liming mechanism are quite complicated. In this study, calcium hydroxide and urea were utilized in liming. The solution pH, hide swelling ratio and non-collagenous protein removal were quantitatively analyzed. The morphologies of both limed and fresh hides were studied by optical microscopy. The reaction mechanism of fiber opening up of cattle hides was analyzed and speculated by the combination of thermogravimetric analysis and Fourier transformation infrared spectroscopy. It was found that the fiber bundles of hides limed by urea/calcium hydroxide have a better opening up effect than that by pure calcium hydroxide. The mechanism of liming in an urea/calcium hydroxide solution system was proposed. Note de contenu : - EXPERIMENTAL : Materials - Liming treatment - pH of the liming solutions - Swelling ratios of cattle hides - Protein content in wastewater - Proteoglycan content in wastewater - Hydroxyproline content in wastewater - Structure
- RESULTS AND DISCUSSION : The pH of liming solutions - Swelling ratio of hides after liming - Contents of total protein proteoglycan and hydroxyproline in wastewater - Histological photographs and scanning electron microscopy - TG results - Possible liming mechanism
- Table 1 : Quantitative evaluation of beamhouse processes
- Table 2 : The onset temperature and weight loss ratio of hides limed with different liming systemsDOI : https://doi.org/10.34314/jalca.v116i5.4290 En ligne : https://drive.google.com/file/d/1aZQ5PRfXiX6tp0ZZbmBHHYtHdlg7Bg6O/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=35757
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Code-barres Cote Support Localisation Section Disponibilité 22726 - Périodique Bibliothèque principale Documentaires Disponible Collagen hydrolysate extraction from chromed leather waste for polymeric film production / Bianca S. Scopel in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXI, N° 1 (01/2016)
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Titre : Collagen hydrolysate extraction from chromed leather waste for polymeric film production Type de document : texte imprimé Auteurs : Bianca S. Scopel, Auteur ; D. L. Lamers, Auteur ; Eric Matos, Auteur ; Camila Baldasso, Auteur ; Aline Dettmer, Auteur Année de publication : 2016 Article en page(s) : p. 30-40 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Amidons
Couches minces
Couches minces -- Propriétés mécaniques
Cuirs et peaux -- Déchets -- Recyclage
Extraction (chimie)
GlycérineLe glycérol, ou glycérine, est un composé chimique de formule HOH2C–CHOH–CH2OH. C'est un liquide incolore, visqueux et inodore au goût sucré, utilisé dans de nombreuses compositions pharmaceutiques. Sa molécule possède trois hydroxyles correspondant à trois fonctions alcool responsables de sa solubilité dans l'eau et de sa nature hygroscopique. Un résidu glycérol constitue l'articulation centrale de tous les lipides de la classe des triglycérides et des phosphoglycérides.
PROPRIETES PHYSIQUES : Le glycérol se présente sous la forme d'un liquide transparent, visqueux, incolore, inodore, faiblement toxique si ingéré (mais laxatif à haute dose), au goût sucré.
Le glycérol peut se dissoudre dans les solvants polaires grâce à ses trois groupes hydroxyles. Il est miscible dans l'eau et l'éthanol ; et insoluble dans le benzène, le chloroforme et le tétrachlorométhane.
Son affinité avec l'eau le rend également hygroscopique, et du glycérol mal conservé (hors dessicateur ou mal fermé) se dilue en absorbant l'humidité de l'air.
- PROPRIETES CHIMIQUES : Dans les organismes vivants, le glycérol est un composant important des glycérides (graisses et huiles) et des phospholipides. Quand le corps utilise les graisses stockées comme source d'énergie, du glycérol et des acides gras sont libérés dans le sang.
- DESHYDRATATION : La déshydratation du glycérol est faite à chaud, en présence d'hydrogénosulfite de potassium (KHSO3) et produit de l'acroléine
- ESTERIFICATION : L'estérification du glycérol conduit à des (mono, di ou tri) glycérides.
- AUTRES PROPRIETES : Le glycérol a un goût sucré de puissance moitié moindre que le saccharose, son pouvoir sucrant est de 0,56-0,64 à poids égal13.
Le glycérol a des propriétés laxatives et diurétiques faibles.
Comme d'autres composés chimiques, tels que le benzène, son indice de réfraction (1,47) est proche de celui du verre commun (~1,50), permettant de rendre "invisibles" des objets en verre qui y seraient plongés.
Hydrolysats de protéines
PolymèresIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : The generation of hazardous wastes and the overuse of nonrenewable sources in polymeric materials production are two major concerns for researchers worldwide. In this paper, an innovative approach to changing chromed leather waste (CLW) into a raw material for polymeric film production was studied. Collagen hydrolysate was extracted from CLW through alkaline hydrolysis. Time, temperature, agitation speed, type and mass of alkalinizing agent were tested. The optimum condition for collagen hydrolysate production (the one that results in a high protein and low chromium content) was determined. According to statistical analysis, hydrolysis performed for 6 h using a proportion of 4 g of MgO for each 50 g of CLW and 250 ml of water at 70°C and 180 rpm of agitation speed led to the best protein/chromium ratio in the collagen hydrolysate (TKN: 2,185.7 mg/L, Cr: <0.04 mg/L). The collagen hydrolysate obtained with optimum condition of production was then mixed with starch - a renewable source for polymeric material production - and glycerol - a byproduct of biodiesel production - to produce polymeric films by casting technique. Mechanical properties of four different compositions (with and without the presence of collagen hydrolysate and glycerol) of films were compared. The films produced with the addition of glycerol and collagen hydrolysate presented mechanical properties similar to the ones of commercial biodegradable films applied as mulches in agriculture. They also have in their composition a compound present in fertilizers - nitrogen - and possible traces of chromium, which is a micronutrient. Therefore, they can be an alternative to synthetic polymers. Note de contenu : - MATERIALS AND METHODS : Materials - Collagen hydrolysate extraction - Film production - Characterization methods
RESULTS AND DISCUSSION : CLW characterization - Collagen hydrolysate extraction - Film productionEn ligne : https://drive.google.com/file/d/1rOz_3-AWwBFBpO5i3u3YYFWRYlTxgpTG/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=25276
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Code-barres Cote Support Localisation Section Disponibilité 17767 - Périodique Bibliothèque principale Documentaires Disponible Collagen modification using nanotechnologies : a review / Deng-Ge Gao in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 10 (10/2013)
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Titre : Collagen modification using nanotechnologies : a review Type de document : texte imprimé Auteurs : Deng-Ge Gao, Auteur ; Jian-Zhong Ma, Auteur ; Bin Lv, Auteur ; Zhang Jing, Auteur Année de publication : 2013 Article en page(s) : p. 392-400 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Argent
Argile
Collagène
Copolymères greffés
Copolymérisation
Dioxyde de silicium
Nanoémulsions
Nanoparticules
NanotechnologieIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : The essence of leather the industry is modified collagen fibers. With more challenges facing traditional chemicals used for leather making, along with the development of higher living standards, great demand is imposed on the leather industry. Therefore, more researchers are paying attention to collagen modification using nanotechnologies for the leather industry. In this review, we present a critical discussion of collagen modified by nano-size emulsion, clay minerals, nano silicon dioxide, or nanosilver. In the end, we conclude this review with some perspectives on the future research and development of collagen modified by nanotechnology. Note de contenu : - NANO-SIZE EMULSIONS
- CLAY MINERALS
- NANO SILICON DIOXIDE : Producing nano-Sio2 between fibers on hide by in-situ method - Graft-copolymerization method - Nano dichromium trioxide
- NANOSILVEREn ligne : https://drive.google.com/file/d/18ISw97m7cbVhsuxVWu5B63AbNLO5vYm7/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=19462
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Code-barres Cote Support Localisation Section Disponibilité 15578 - Périodique Bibliothèque principale Documentaires Disponible Collagen - A natural scaffold for biology and engineering / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIV, N° 8 (08/2009)
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Titre : Collagen - A natural scaffold for biology and engineering Type de document : texte imprimé Auteurs : Eleanor M. Brown, Auteur Année de publication : 2009 Article en page(s) : p. 275-285 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Collagen, the most abundant protein in mammals, constitutes a quarter of the animal's total weight. The unique structure of fibrous collagens, a long triple helix that further associates into fibers, provides an insoluble scaffold that gives strength and form to the skin, tendons, bones, cornea and teeth. The ready availability, to meat eaters, of animal skins that would putrefy, if left untreated, led to man's earliest venture into biomaterials engineering and resulted in the production of leather. Through empirical methods, a number of tanning agents with a variety of properties were identified. The methods for production of leather evolved over several centuries as art and engineering with little understanding of the underlying science. Scientific advances of the twentieth century, including increasing use of collagen in medical biomaterial research, began to provide a basis for understanding the relationship between collagen structure and function in both biology and technology. During the past 20 years, leather researchers at ERRC have used experimental and theoretical approaches to investigate several methods for stabilizing collagen structure. This research, which includes studies of mineral and vegetable tannages, enzyme-catalyzed and aldehyde-based covalent crosslinks, electrostatic and hydrophobic interactions, will be reviewed. Insight gained from these studies and those of other leather and biomaterials scientists will be evaluated as steps toward a still elusive, comprehensive mechanism for stabilization of collagen in leather and other biomaterials. En ligne : https://drive.google.com/file/d/1IvTrzerw5QFp4V6L2oJ8BfpkT5nYVpAP/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=6094
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Code-barres Cote Support Localisation Section Disponibilité 011496 - Périodique Bibliothèque principale Documentaires Disponible Collagen : a not so simple protein / A. J. Bailey in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 82, N° 3 (05-06/1998)
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Titre : Collagen : a not so simple protein Type de document : texte imprimé Auteurs : A. J. Bailey, Auteur ; R. G. Paul, Auteur Année de publication : 1998 Article en page(s) : p. 104-110 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène
Cuirs et peauxIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Collagen is the major protein of animal bodies from simple sponges to homo sapiens and exists in various froms from skin, tendon and bone to cornea and basement membrane of the capillaries. This biological variation can now be accounted for on the basis of a whole family of genetically distinct collagens. OVer the past two decades 19 different collagens have been identified, although the major types are the fibrous types I, II and III and the non-fibrous type IV of basement membrane. They all possess the basic triple helix based on multiple repeats of the simple tri-peptide Gly-W-Y, but this varies in length and forms different supramolecular aggregates to achieve optimum function for particular tissues. The major function of collagenis to provide shape and mechanical strength and the latter is achieved by intermolecular crosslinking of the collagen molecules in the supramolecular aggreate. The monomeric molecules in the aggregates are stabilised by two different pathways. Initially cross-linking occurs through an enzymic mechanism involving oxidation of specific lysine and hydroxylysine residues providing divalent cross-linking which subsequently matures to multivalent cross-links. As the rate of turnover decreases a non-enzymic pathway takes over, which is mediated throug the adventitious accretion of glucose. Collagen therefore, unlike other proteins shows considerable changes with age which in turn affect its physical properties. These changes must be taker into accoung when preparing collagen based products ?
All the amino acid side chains project radially for the rod-like triple helix and the quarter-staggered array of the molecules allows highly specific intermolecular cross-linking either naturally, or artificially with bifunctional reagents. Reactions with basic or acid groups can therefore be carefully controlled and in some case their location predicted. Synthetic cross-links bind the molecules closer together and increase intermolecular interactions, thus increasing the shrinkage temerature and resistance to enzymic degradation.
The turnover of collagen is generally slow but in fact can vary from 2/3 days for periodontal ligament to several years for skin and tendon. Mature collagen fibres arehighly resistant to enzymes and degradation is achieved by specific collagenase that can cleave the triplehelix at one particular point. The shorter helical fragments can then unravel and denature to gelatin when ogher metalloproteinases (MMPs) degrade it to amino acids. A family of 14 metalloproteinases have been identified along with some specific tissue inhibitors (TIMPS).
The sharp denaturation temperature of collagen attests to the almost crystalline character of the triple helix and the variation in shrinkage temperature between species is primarily due to the number of hydroxyproline based water hydrogen bridges. The presence of a hydroxyproline deficient thermally labile domain near the carboxy terminus of the molecule initiates the melting process allowing the triple helix to unzip along its length.
Recent studies have demonstrated that collagen is not an inert structural material but interacts with other molecules to control the development of collagenous tissues. Despite the ancient lineage of this ubiquitous protein, collagen is still revealing exciting new scientific features.Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=7903
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Code-barres Cote Support Localisation Section Disponibilité 007022 - Périodique Bibliothèque principale Documentaires Disponible Collagen processing / Gennaro J. Maffia in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCIX, N° 4 (04/2004)
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PermalinkCollagen D-spacing and the effect of fat liquor addition / Katie H. Sizeland in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 3 (03/2015)
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PermalinkCollagen structure changes during chrome tanning in propylene carbonate / Yi Zhang in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 1 (Année 2019)
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PermalinkCollagen thermal transitions in chrome leather - thermogravimetry and differential scanning calorimetry / Teresa Bosch in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 11 (11/2002)
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PermalinkCollagen utilization / Valerie A. Lipsett in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXV (Année 1980)
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PermalinkPermalinkCollection cuirs / Nathalie Hustache Mathieu / Lyon : Centre Technique Cuir, chaussure, maroquinerie (CTC) (2016)
PermalinkColor control for the leather industry / L. Jay Sidney in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXVI, N° 10 (10/1991)
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PermalinkColor measurement and control in leather education committee invited lecture / Daniel L. Randall in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXIX, N° 10 (10/1994)
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PermalinkLes colorants métallifères et leurs applications dans l'industrie du cuir / François Grall in TECHNICUIR, N° 2 (02/1975)
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PermalinkColorants solides au lavage et au nettoyage / Wilhelm Pauckner in REVUE TECHNIQUE DES INDUSTRIES DU CUIR, Vol. LXVI (Année 1974)
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PermalinkPermalinkColorimetric assessment of wool fabric staining as a model for studying reduction of chromium staining during tanning of woolly sheepskins / L. J. Stephens in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 67 (Année 1983)
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PermalinkPermalinkColoring of leather using henna - natural alternative material for dyeing / A. E. Musa in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIV, N° 5 (05/2009)
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PermalinkColoring sheepskins / Raymond Hart in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXIV (Année 1989)
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PermalinkColour and gloss properties of pigment-printed synthetic leather using an ultraviolet-curable water-borne polyurethane acrylate binder and two photoinitiators at different ratios / Gülçin Baysal in COLORATION TECHNOLOGY, Vol. 135, N° 2 (04/2019)
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PermalinkColour changes during ageing of finished leather / H. Turner in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 5 (09-10/1992)
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PermalinkColour changes in wet blue leathers / J. R. Barlow in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 60 (Année 1976)
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PermalinkColour changes in wet blue leathers / John R. Barlow in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 60, N° 6 (11-12/1976)
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