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Recent advances in skin collagen : functionality and non-medical applications / Yanting Han in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 3 (Année 2021)
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Titre : Recent advances in skin collagen : functionality and non-medical applications Type de document : texte imprimé Auteurs : Yanting Han, Auteur ; Jinlian Hu, Auteur ; Gang Sun, Auteur Année de publication : 2021 Article en page(s) : 12 p. Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Adsorption
Blindage (électricité)
Collagène
Eau -- Epuration
Effet mémoire de forme
Electronique -- Matériaux
Imperméabilisation
Matériaux intelligents
Matrices
Peau artificielleIndex. décimale : 611.78 Peau et ongles Résumé : During nature evolution process, living organisms have gradually adapted to the environment and been adept in synthesizing high performance structural materials at mild conditions by using fairly simple building elements. The skin, as the largest organ of animals, is such a representative example. Conferred by its intricate organization where collagen fibers are arranged in a randomly interwoven network, skin collagen (SC), defined as a biomass derived from skin by removing non-collagen components displays remarkable performance with combinations of mechanical properties, chemical-reactivity and biocompatibility, which far surpasses those of synthetic materials. At present, the application of SC in medical field has been largely studied, and there have been many reviews summarizing these efforts. However, the generalized view on the aspects of SC as smart materials in non-medical fields is still lacking, although SC has shown great potential in terms of its intrinsic properties and functionality. Hence, this review will provide a comprehensive summary that integrated the recent advances in SC, including its preparation method, structure, reactivity, and functionality, as well as applications, particularly in the promising area of smart materials. Note de contenu : - Preparation of SC
- Structure of SC
- Modification of SC
- Advanced properties and non-medical applications : Water treatment - Biotemplate - Wave-adsorbing/shielding - Shape memory - Waterproof - Electronic skin
- Table 1 : Modification agents for SCDOI : https://doi.org/10.1186/s42825-020-00046-9 En ligne : https://link.springer.com/content/pdf/10.1186/s42825-020-00046-9.pdf Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37465
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 3 (Année 2021) . - 12 p.[article]Recent strategies of collagen-based biomaterials for cartilage repair : from structure cognition to function endowment / Xiaoyue Yu in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 4 (Année 2022)
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Titre : Recent strategies of collagen-based biomaterials for cartilage repair : from structure cognition to function endowment Type de document : texte imprimé Auteurs : Xiaoyue Yu, Auteur ; Haiping Zhang, Auteur ; Yiliang Miao, Auteur ; Shanbai Xiong, Auteur ; Yang Hu, Auteur Année de publication : 2022 Article en page(s) : 23 p. Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Biopolymères
Cartilage
Collagène
Ingénierie tissulaire
Polymères en médecine
Régénération (biologie)Index. décimale : 668.9 Polymères Résumé : Collagen, characteristic in biomimetic composition and hierarchical structure, boasts a huge potential in repairing cartilage defect due to its extraordinary bioactivities and regulated physicochemical properties, such as low immunogenicity, biocompatibility and controllable degradation, which promotes the cell adhesion, migration and proliferation. Therefore, collagen-based biomaterial has been explored as porous scaffolds or functional coatings in cell-free scaffold and tissue engineering strategy for cartilage repairing. Among those forming technologies, freeze-dry is frequently used with special modifications while 3D-printing and electrospinning serve as the structure-controller in a more precise way. Besides, appropriate cross-linking treatment and incorporation with bioactive substance generally help the collagen-based biomaterials to meet the physicochemical requirement in the defect site and strengthen the repairing performance. Furthermore, comprehensive evaluations on the repair effects of biomaterials are sorted out in terms of in vitro, in vivo and clinical assessments, focusing on the morphology observation, characteristic production and critical gene expression. Finally, the challenge of biomaterial-based therapy for cartilage defect repairing was summarized, which is, the adaption to the highly complex structure and functional difference of cartilage. Note de contenu : - STRUCTURE AND DEFECTS OF CARTILAGE : The composition of articular cartilage - Hierarchical structure of articular cartilage - The etiology and degree of cartilage defect - Current repair strategies - - STRUCTURE AND FUNCTION OF COLLAGEN : Hierarchical structure of COL I - The role of COL I in cartilage repair
- DESIGN AND PREPARATION OF COLLAGEN-BASED BIOMATERIALS FOR CARTILAGE DEFECT REPAIR : Forming and cross-linking of collagen-based biomaterials - Incorporated fabrication of collagen-based biomaterials for cartilage repair
- COMPREHENSIVE EVALUATIONS OF CARTILAGE REPAIR BY COLLAGEN-BASED BIOMATERIALS : Physicochemical properties - Bioactivities for cartilage repair - Clinical diagnosis
- Table 1 : General methods used to evaluate the bioactivities of biomaterialsDOI : https://doi.org/10.1186/s42825-022-00085-4 En ligne : https://link.springer.com/content/pdf/10.1186/s42825-022-00085-4.pdf Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37578
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 4 (Année 2022) . - 23 p.[article]Recherches concernant la réaction de certains amino-acides du collagène avec les sels de zirconium / valeriu Nanescu in REVUE TECHNIQUE DES INDUSTRIES DU CUIR, Vol. LXIV (Année 1972)
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Titre : Recherches concernant la réaction de certains amino-acides du collagène avec les sels de zirconium Type de document : texte imprimé Auteurs : valeriu Nanescu, Auteur ; Georges Alexa, Auteur Année de publication : 1972 Article en page(s) : p. 6-17 Note générale : Bibliogr. Langues : Français (fre) Catégories : Acides aminés Les acides aminés (ou aminoacides) sont une classe de composés chimiques possédant deux groupes fonctionnels : à la fois un groupe carboxyle –COOH et un groupe amine –NH2. Parmi ceux-ci, les acides α-aminés se définissent par le fait que leur groupe amine est lié à l'atome de carbone adjacent au groupe acide carboxylique (le carbone α), ce qui leur confère la structure générique H2N–CHR–COOH, où R représente la chaîne latérale, qui identifie l'acide α-aminé.
Les acides α-aminés jouent un rôle fondamental en biochimie comme constituants élémentaires des protéines : ils polymérisent en formant des liaisons peptidiques qui aboutissent à de longues chaînes macromoléculaires appelées peptides.
Chlorure de zirconyleLe chlorure de zirconyle, ou oxychlorure de zirconium, est un composé chimique de formule ZrOCl2, presque toujours sous forme d'octahydrate ZrOCl2·8H2O. Il se présente sous la forme d'un solide blanc et est le dérivé hydrosoluble du zirconium le plus courant. Sa structure est organisée autour du cation [Zr4(OH)8]8+ avec quatre paires d'anions hydroxyde HO– pontants entre quatre centres Zr+. Les anions chlorure Cl– ne sont pas des ligands, ce qui est cohérent avec la nature très oxophile du cation Zr4+.
Il peut être obtenu en hydrolysant du chlorure de zirconium(IV) ZrCl4 ou en traitant du dioxyde de zirconium ZrO2 avec de l'acide chlorhydrique HCl.
Collagène
Conductimétrie
Réactions chimiquesIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : On sait que par l'arrangement des amino-acides de la structure du collagène ils restent sous forme de points réactifs, les mêmes groupes chimiques comme ceux qui se trouvent dans les amino-acides.
La réaction des amino-acides avec les sels métalliques, a indiqué leur caractère de ligands bicoordonnés.
Jusqu'à 1950, la préoccupation pour les substances résultant de la réaction des amino-acides et les sels métalliques, a été axé seulement sur la préparation de ces substances mais, ultérieurement on en a fait des études pour déterminer leur structure et leur stabilité.
Parallèlement, avec les études des substances tannantes concernant leurs aspects technico-scientifiques, on en a fait des investigations pour expliquer le mécanisme de réaction d'entre les groupes réactives du collagène et les tanins.
La consultation de la littérature spécialisée, en ce qui concerne le mécanisme de réaction des sels de zirconium et le collagène, fait ressortir qu'il existe des aspects qui n'ont pas été suffisamment élucidés.En ligne : https://drive.google.com/file/d/1WtEqMEvnePDoQomkz5_waE9Be40aATYz/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=36724
in REVUE TECHNIQUE DES INDUSTRIES DU CUIR > Vol. LXIV (Année 1972) . - p. 6-17[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 008571 - Périodique Bibliothèque principale Documentaires Disponible Recovery and characterization of protein hydrolysate from chrome shavings by microbial degradation / C. Shanthi in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 6 (06/2013)
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Titre : Recovery and characterization of protein hydrolysate from chrome shavings by microbial degradation Type de document : texte imprimé Auteurs : C. Shanthi, Auteur ; Pradipta Banerjee, Auteur ; Chandra Babu Narasimhan Kannan, Auteur ; G. Suseela Rajkumar, Auteur Année de publication : 2013 Article en page(s) : p. 231-239 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Bactéries
Biodégradation
Caractérisation
Collagène
Cuirs et peaux -- Déchets -- Recyclage
Hydrolysats de protéines
Récupération (Déchets, etc.)Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Chromium containing collagenous solid wastes from the leather tanning industry requires special attention because of the pressure exerted by environmental authorities for safe disposal. Such collagen-rich wastes can be recycled by adapting environmentally suitable and safer methods based on microorganism and/or enzymatic treatment, so as to obtain a collagen hydrolysate with potential applications. In the present study, chromium tolerant bacteria were isolated from tannery soil and screened for high proteolytic activity by zone-clearance assay and caseinolytic activity. The most potent bacterium, with a high proteolytic and chromium-tolerant ability was found to degrade about 90% of the chrome shavings in 120h and was identified as Alcaligenes faecalis. The hydrolysates at various time intervals of proteolysis were collected, chromium removed and characterized. The hydrolysate was found to have 12% ash and 80% protein or peptides contents after 120h of proteolysis with 3.14±2.0?g of chromium/g of protein. Molecular weight profiling done by gel filtration chromatography using sephadex G 25 and tricine-SDS-PAGE electrophoresis revealed that the major component of the hydrolysate comprised of small peptides in the molecular weight range of 3-30kDa. Note de contenu : - MATERIALS AND METHODS : Isolation of organism - Protease activity - Chromium tolerance - Degre of hydrolysis (%) and Cr3 removal from the chrome shavings - Analysis of the protein hydrolysate - pH determination by deionization - Gel filtration chromatography - Ion exchange chromatography - Tricine SDS-PAGE of the hydrolysate
- RESULTS AND DISCUSSION : Protease activity, identification and chromium tolerance of the screened bacterium - Chrome shaving hydrolysis process - Characterization of protein hydrolysate - Determination of molecular weight of protein hydrolysate by gel filtration and gel electrophoresisEn ligne : https://drive.google.com/file/d/1LQ3kblknV4gm5BdYm3xIrye-aspbynzD/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=18746
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CVIII, N° 6 (06/2013) . - p. 231-239[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 15158 - Périodique Bibliothèque principale Documentaires Disponible Recovery of collagen from phosphonium tanned leather shavings and application as formaldehyde scavenger in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIV, N° 9 (09/2009)
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Titre : Recovery of collagen from phosphonium tanned leather shavings and application as formaldehyde scavenger Type de document : texte imprimé Année de publication : 2009 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Capteurs chimiques
Collagène
Cuirs et peaux -- Déchets -- Recyclage
Formaldéhyde
Formaldéhyde -- EliminationIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Samples of collagen extracted from phosphonium tanned leather shavings by three different methods (acid, alkali, magnesium oxide dissolution and alkaline protease hydrolysis treatments) were characterized with respect to their components and morphology of fibril network. The ratio of collagen gained was 90% by the process of alkali dissolution and enzyme hydrolysis, which was much higher than that of acid and alkali methods. The results from amino acid analysis showed that the components of extracted collagen were similar with that of commercial gelatin. The Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) results indicated that the extracted substance was the mixture of polypeptide and amino acid. The polypeptide and amino acid exposed to hydrophilic functional groups including carboxyl, hydroxyl, amino group etc. These functional groups especially amino group can react with formaldehyde which leads to scavenge formaldehyde. The morphological change of leather shavings treated by magnesium oxide and alkaline protease was clearly presented with scanning electron microscope. The percentage of formaldehyde removal and thickening rate of collagen were 51.8% and 10.4%, respectively. Therefore, the collagen from the leather shavings and used as the formaldehyde scavenger has a good potential in achieving the innocent treatment and reuses of the solid leather wastes. En ligne : https://drive.google.com/file/d/1yE-gqcl5axgFcpVPlYQwE85efCOch21E/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=17836
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CIV, N° 9 (09/2009)[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 011556 - Périodique Bibliothèque principale Documentaires Disponible 011557 - Périodique Bibliothèque principale Documentaires Disponible Recovery of collagen hydrolysate from chrome leather shaving tannery waste through two-step hydrolysis using magnesium oxide and bating enzyme / Alvin Asava Sasia in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 103, N° 2 (03-04/2019)
PermalinkRecycling of raw materials (collagen protein) in the leather industry -high value added application of leather solid waste / Li Chengtao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 101, N° 5 (09-10/2017)
PermalinkRedox proteomic evaluation of oxidative modification and recovery in a 3D reconstituted human skin tissue model exposed to UVB / J. M. Dyer in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 39, N° 2 (04/2017)
PermalinkRegenerating leather waste for flexible pressure sensing applications / Jie Lei in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 1 (Année 2019)
PermalinkRenewing skin from the heart of the dermis / Sonia Léglise in GLOBAL PERSONAL CARE, Vol. 22, N° 6 (06/2021)
PermalinkResearch on thermal stability, moisture and air permeability of natural leather based on the spatial conformation of the type 1 collagen molecule / Zhong Anhua in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 101, N° 5 (09-10/2017)
PermalinkResource utilisation of solid leather waste - Part I / Shyamoli Shaw in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 106, N° 3 (05-06/2022)
PermalinkRheological behaviour of alkali solubilized collagen from limed bovine split wastes / Chen Yihui in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 97, N° 5 (09-10/2013)
PermalinkSalt-pH effects on collagen thermal stability in pickling and curing / A. E. Russel in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 59 (Année 1975)
PermalinkSalt-pH effects on collagen thermal stability in pickling and curing / A. E. Russel in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 59, N° 1 (01-02/1975)
PermalinkSoy protein isolate reinforced yak skin collagen edible films for ultraviolet barring function / Ruirui Wang in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 103, N° 4 (07-08/2019)
PermalinkStabilized green tea polyphenols protecting skin from pollution / Marlène De Matos in SOFW JOURNAL, Vol. 143, N° 1/2 (01-02/2018)
PermalinkStrengthening natural protection against light / Sonia Léglise in PERSONAL CARE EUROPE, Vol. 14, N° 2 (04/2020)
PermalinkStructural changes in dermal collagen and oxidative stress levels in the skin of Japanese overweight males / M. Matsumoto in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 36, N° 5 (10/2014)
PermalinkStructure and properties of a novel collagen-soy protein isolate film via self-assembly : a comparative study / Ruirui Wang in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 104, N° 1 (01-02/2020)
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