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Auteur Maryann M. Taylor
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United States Department of Agriculture, Agricultural Research Service Eastern Regional Research Center - Mermaid Lane, Wyndmoor, PA - USA
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Taylor, M. M.
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Efficiency of enzymic solubilization of chrome shavings as influenced by choice of alkalinity-inducing agents / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXVI, N° 6 (06/1991)
[article]
Titre : Efficiency of enzymic solubilization of chrome shavings as influenced by choice of alkalinity-inducing agents Type de document : texte imprimé Auteurs : Maryann M. Taylor, Auteur ; Edward J. Diefendorf, Auteur ; William N. Marmer, Auteur Année de publication : 1991 Article en page(s) : p. 199-209 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : Enzymic processing of chrome shavings has been shown to be a viable treatment of this waste product. Proteolytic enzymes, active at moderate temperatures, are effective in solubilizing the protein and, since the reaction takes place at an alkaline pH, the chromium remains insoluble. Various alkalinity-inducing agents, such as magnesium oxide, alone or in combination with calcium hydroxide, sodium hydroxide or sodium carbonate, can be employed to maintain the optimal environment for enzyme hydrolysis. These systems can be tailored to match the varied chrome-recycling steps that different tanneries employ. Some of these systems have improved the rate of solubilization of the shavings while lowering the required amount of enzyme, thus making the process more cost-effective. En ligne : https://drive.google.com/file/d/1tDRf8LxiIA6RBi8a5d7LW4sqtIsZD_5N/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8494
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXXXVI, N° 6 (06/1991) . - p. 199-209[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 006881 - Périodique Bibliothèque principale Documentaires Disponible Enzymatic modification of hydrolysis products from collagen using a microbial transglutaminase. I. Physical properties / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVI, N° 9 (09/2001)
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Titre : Enzymatic modification of hydrolysis products from collagen using a microbial transglutaminase. I. Physical properties Type de document : texte imprimé Auteurs : Maryann M. Taylor, Auteur ; Luisa F. Cabeza, Auteur ; William N. Marmer, Auteur ; Eleanor M. Brown, Auteur Année de publication : 2001 Article en page(s) : p. 319-332 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : In previously reported research from this laboratory, gelatins, both commercial and experimental of varying gel strengths, were chemically modified using glutaraldehyde, glyoxal, and carbodiimide. These classical modifications effectively changed the physical and functional properties of gelatin; however, they have drawbacks in that the crosslinking agents are potentially toxic. Transglutaminase is an enzyme capable of forming inter- or intra-molecular cross-links in many proteins. The enzyme catalyzes an acyl transfer reaction between the g-carboxamide group of peptide-bound glutamine residues as acyl donors and primary amines as acceptors. When the e-amino group of peptide-bound lysine acts as acyl acceptor, an e-(g-glutamyl) lysine cross-link is formed. This enzyme, now isolated by fermentation, is commercially available, relatively inexpensive, and environmentally safe. We modified gelatins of varying quality with microbial transglutaminase. Gel strengths of low bloom gelatins improved with increasing enzyme concentrations, whereas the gel strengths of higher bloom gelatins either remained the same or decreased with increasing enzyme concentrations. All gelatins gave higher melting points with increasing amounts of enzyme, some even higher than 90ºC. Viscosities, measured at 60ºC and at or near room temperature, increased with increasing enzyme concentrations. The temperature of gelation, as described in the literature, increased not only with the quality of the gelatin but also with increasing enzyme concentrations. Potential applications for this enzyme in by-product utilization and possibly the leather-making process are numerous. En ligne : https://drive.google.com/file/d/1wvenobFOzHHSyBVxHpPVwLjdWfOQ9qxk/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4363
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Code-barres Cote Support Localisation Section Disponibilité 001566 - Périodique Bibliothèque principale Documentaires Disponible 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)
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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 : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4291
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Code-barres Cote Support Localisation Section Disponibilité 001575 - 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 Enzymatic treatment of offal from fleshing machines / M. M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXIV (Année 1989)
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Titre : Enzymatic treatment of offal from fleshing machines Type de document : texte imprimé Auteurs : M. M. Taylor, Auteur ; Edward J. Diefendorf, Auteur ; T. A. Foglia, Auteur ; David G. Bailey, Auteur ; Stephen H. Feairheller, Auteur Année de publication : 1989 Article en page(s) : p. 71-78 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Cuirs et peaux -- Déchets -- Recyclage
Echarnage
Enzymes protéolytiquesUne enzyme protéolytique est une enzyme capable de couper une protéine en plusieurs fragments ou peptides. La trypsine, la papaïne, la pepsine, la chymotrypsine, la plasmine, la subtilisine... sont capables de couper une protéine, chaque enzyme étant spécifique de certains sites particuliers de cette protéine. C'est ainsi, par exemple, qu'une immunoglobuline G est découpée par la papaïne en un fragment Fc et deux fragments Fab, comme l'a montré Porter en 1959.
Extraction (chimie)
Huiles et graissesIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Pigskin and cattlehide fleshings were treated with four commercially available proteolytic enzymes that had optimal activities at a neutral or alkaline pH. The digestions were carried out at 40°C for 3 hours and then at 60°C for 1 hour. Up to 87% of the available fat was recovered as well as a readily separated protein hydrolyzate fraction. Chemical analysis demonstrated that the fat contained 0,2-6,0% free fatty acid content depending on the treatment. The results suggest that with a small investment in enzymes a good quality fat can be produced from fleshings which will convert a solid waste disposal problem into a value-added by-product. Note de contenu : - Table I : Characterization of fat isolated from pigskin fleshings
- Table II : Effect of time at 60°C on separation of fat from protein
- Table III : Characterization of fat isolated from cattlehide fleshings
- Table IV : Composition of pigskin fleshings
- Table V : Effect of time and treatment on recovery of fat and protein from pigskin fleshings
- Table VI : Treatment of pigskin fleshings with commercial enzymesEn ligne : https://drive.google.com/file/d/1r-UqrGo2NWahQlYH927RyffnHbP63b_3/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=17289
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Code-barres Cote Support Localisation Section Disponibilité 008089 - Périodique Bibliothèque principale Documentaires Disponible Enzymic treatment of chrome shavings / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXV (Année 1990)
PermalinkEssential chromium ? / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVIII, N° 10 (10/2003)
PermalinkEvaluation of polymers prepared from gelatin and casein or whey as potential fillers / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CII, N° 4 (04/2007)
PermalinkExtraction of value added byproducts from the treatment of chromium containing collagenous leather industry waste / Maryann M. Taylor in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 81, N° 1 (01-02/1997)
PermalinkFunctional properties of hydrolysis products from collagen / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCIII, N° 2 (02-03/1998)
PermalinkGenipin -aluminium or -vegetable tannin combinations on hide powder / Keyi Ding in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CII, N° 5 (05/2007)
PermalinkGraft polymerization. IV. Further studies of the initiation step in the graft polymerization of vinyl monomers onto chrome-tanned collagen / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXII (Année 1977)
PermalinkGraft polymerization. IX. Improved distribution of grafted polymers in side leather / M. M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXVI (Année 1981)
PermalinkGraft polymerization VII. Novel source of reductant for graft polymerization of leather / E. H. Harris in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXV (Année 1980)
PermalinkInfluence of pepsin and trypsin on chemical and physical properties of isolated gelatin from chrome shavings / Luisa F. Cabeza in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCII, N° 8 (10/1997)
PermalinkIsolation of protein products from chromium-containing leather waste using two consecutive enzyme and purification of final chromium product : pilot plant studies / Luisa F. Cabeza in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 83, N° 1 (01-02/1999)
PermalinkModified collagen hydrolysate, potential for use as a filler for leather / Wuyong Chen in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVI, N° 7 (07/2001)
PermalinkMolecular size and conformation of protein recovered from chrome shavings / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXIX, N° 7 (07/1994)
PermalinkMolecular weight distribution and functional properties of enzymatically modified commercial and experimental gelatins / Maryann M. Taylor in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCIX, N° 3 (03/2004)
PermalinkNon-ammonia deliming of cattle hides with magnesium lactate / Karel Kolomaznik in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXXI, N° 1 (01/1996)
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