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High exhaust chrome tanning using fleshing hydrolysate / James Kanagaraj in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 6 (06/2002)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCVII, N° 6 (06/2002) . - p. 207-224 Titre : High exhaust chrome tanning using fleshing hydrolysate Type de document : texte imprimé Auteurs : James Kanagaraj, Auteur ; N. Samivelu, Auteur ; Md. Rafiuddin Ahmed, Auteur ; R. Jayakumar, Auteur Année de publication : 2002 Article en page(s) : p. 207-224 Note générale : bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : Fleshing hydrolysate (FH) was prepared from limed fleshings by an alkali digestion method. The FH that was obtained was in the molecular weight range of 15,000 daltons. It was used as a chrome exhaustion aid in chrome tanning and rechroming processes. Various studies on treated cow sides such as percent exhaustion of chromium, shrinkage temperature, strength properties, and scanning electron micrograph studies were carried out in comparison with control samples. The results showed that chromium uptake of the leather was increased by 10 - 20% in the sides treated with FH and the physical properties were comparable to the control samples. En ligne : https://drive.google.com/file/d/1ZJbdSQp5eWgKRaNfZzxb9wStgbivdgfQ/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4289 [article]

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Microemulsion solutions of acrylic copolymers for retanning applications on chrome tanned goat skins / G. Mallikajun in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 6 (06/2002)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCVII, N° 6 (06/2002) . - p. 215-224 Titre : Microemulsion solutions of acrylic copolymers for retanning applications on chrome tanned goat skins Type de document : texte imprimé Auteurs : G. Mallikajun, Auteur ; P. Saravanan, Auteur ; G. V. Ramana, Auteur Année de publication : 2002 Article en page(s) : p. 215-224 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : The tercopolymer microemulsion (M.E.) solutions of methyl methacrylate (MMA), n-butyl acrylate (BA) and methacrylic acid (MAA) are prepared with four different compositions, by employing sodium lauryl sulphate (SLS) and n-pentanol (PA) as surfactant and co-surfactant, respectively, and by using potassium persulphate (KPS) as free radical initiator at a temperature of 70°C. The experimental products are employed in retanning chrome tanned goatskins along with the fatliquoring agent, Vernaminol liquor ASN. The offer of the experimental products are varried in the retanning experiments and the effects of these products on retanned goat skins are observed by measuring tensile strength, tearing strength and bursting strength. The experimental products show marked improvement in these properties. The scanning electron microscopic (SEM) studies are carried out on the retanned leathers retanned by application of microemulsion copolymer solutions prepared with 10 and 15 % of MAA, respectively, in the initial feeds of the microemulsion copolymerization experiments. The SEM analysis shows good filling and retanning effect with the experimental product containing the maximum MAA units in the copolymer under present study. The differential scanning calorimetric (DSC) studies of the retanned leathers retanned by employing the experimental products prepared with 10 and 15 percents of MAA units in the initial feeds of the microemulsion copolymerizations show the endothermic processes, respectively, at 105 and 118°C, which indicates higher shrinkage temperature by the application of the experimental product containing more MAA units (15%) in the copolymer and good retanning ability of the product. En ligne : https://drive.google.com/file/d/1jdLAWCGVLQQw90zMGCvZPJvfq-PVPi5h/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4290 [article]

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Enzymatic modification of hydrolysis products from collagen using a microbial transglutaminase. II. Preparation of films / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 6 (06/2002)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCVII, N° 6 (06/2002) . - p. 225-234 Titre : Enzymatic modification of hydrolysis products from collagen using a microbial transglutaminase. II. Preparation of films Type de document : texte imprimé Auteurs : Maryann M. Taylor, Auteur ; Cheng-Kung Liu, Auteur ; Nicholas P. Latona, Auteur ; William N. Marmer, Auteur ; Eleanor M. Brown, Auteur Année de publication : 2002 Article en page(s) : p. 225-234 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : The use of renewable resources in the production of goods traditionally made from petroleum products has recently gained increasing research interest. Environmental concerns, such as biodegradability and ever increasing landfill fees, could be allayed by use of these products. During the conversion of hides and skins into leather, a high percentage of the original collagen substrate becomes waste. This waste has potential for recycling into useful products. Historically, gelatins (a collagen by-product) have been modified chemically, and the physical properties of these products have been improved. However, because of cost and the toxicity issues associated with some crosslinking chemicals, enzymatically modified products would be highly desirable. Commercial gelatins were treated enzymatically with a microbial transglutaminase, mixed with glycerol as plasticizer, and films were prepared. It was found that the amount of glycerol added affected the mechanical properties, particularly the maximum strain. Increasing the concentration of cross-linking agent gave products with higher tensile strengths that were less soluble in water and had improved water absorption properties. The products resulting from these studies have implications not only in the preparation of edible films and sausage casings, but also in the packaging material market, a market not previously utilized because of poor mechanical properties of gelatin films. En ligne : https://drive.google.com/file/d/1su4LsTGTT8SqZfWaqGbeArqyVz3oJwhB/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4291 [article]

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Molecular modeling of N-terminal telopeptides of bovine type I collagen / Phoebe X. Qi in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 6 (06/2002)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCVII, N° 6 (06/2002) . - p. 235-243 Titre : Molecular modeling of N-terminal telopeptides of bovine type I collagen Type de document : texte imprimé Auteurs : Phoebe X. Qi, Auteur ; Eleanor M. Brown, Auteur Année de publication : 2002 Article en page(s) : p. 235-243 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Functionality, both biological and technological, follows from protein structure. Computer-assisted molecular modeling is a useful tool for visualizing structure-function relationships in proteins. A model of the triple helical portion of a bovine type I collagen microfbril was previously developed in our laboratory for use in studies of mechanisms of collagen crosslinking and modification. This model has now been enhanced by the addition of the N-terminal, nonhelical, telopeptides. The telopeptide region is highly flexible, allowing reactive side-chains of residues such as lysine to assume conformations favorable for interaction with adjacent triple helix chains. All naturally occurring collagen crosslinks are anchored in the telopeptide region. This enhancement to our model will enable us to visualize the effects of enzymatic crosslinking on collagen structure and stability. The current model is now more useful for studying mechanisms of inter- and intramicrofibril crosslinking of collagen by chemical and biochemical methods. The potential for transglutaminase crosslinking of collagen is explored with the model. En ligne : https://drive.google.com/file/d/1fyvNuAYfLxmLsoCIHZYmi-Oin2CYU_Oo/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4292 [article]

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