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Collagen processing / Gennaro J. Maffia in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCIX, N° 4 (04/2004)
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Titre : Collagen processing Type de document : texte imprimé Auteurs : Gennaro J. Maffia, Auteur ; Eleanor M. Brown, Auteur ; Peter H. Cooke, Auteur ; M. A. Seltzer, Auteur Année de publication : 2004 Article en page(s) : p. 164-169 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Collagen dispersions, produced from fibrils recovered from milled bovine collagen, have shown promise in environmental remediation in applications as settling aids, filtration aids, fractionation media, oil drop stabilizers, and water purification aids. Macroporous structures, processed by controlled lyophilization of collagen dispersions, are suitable as cell culturing substrates. Collagen was structurally characterized during milling to assist in designing a method for scale-up of the production process. In fact, although the initial processing involves a ball mill, the actual operation is more of an unraveling of the fiber to expose the fibrils, which have nanoscale dimensions. During the ball-milling step of production the active surface area of the collagen increases more than 200 times without chemically altering or denaturing the collagen. To demonstrate this throughout the milling process, active surface area per mass, fibril structure, molecular weight distribution, percent lipid, percent nitrogen, and percent ash were monitored. En ligne : https://drive.google.com/file/d/1zuNakelG5Lys4nCDSoLvZepplFoNnqBQ/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4190
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCIX, N° 4 (04/2004) . - p. 164-169[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 001600 - Périodique Bibliothèque principale Documentaires Disponible 001601 - Périodique Bibliothèque principale Documentaires Disponible A comparison of chemical, physical and enzymatic crosslinking of bovine type I collagen fibrils / Andrew Lastowka in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. C, N° 5 (05/2005)
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Titre : A comparison of chemical, physical and enzymatic crosslinking of bovine type I collagen fibrils Type de document : texte imprimé Auteurs : Andrew Lastowka, Auteur ; Gennaro J. Maffia, Auteur ; Eleanor M. Brown, Auteur Année de publication : 2005 Article en page(s) : p. 196-202 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Insoluble type I collagen fibrils are used in several biotechnological research applications including artificial organ scaffolding, skin grafts and cell immobilization beads for fluidized bed reactors. In these applications, collagen is usually strengthened against enzymatic degradation and physical stresses by the addition of cross-links. A suitable collagen source for these purposes appears to be bovine corium, from the lower split of a fleshed hide, a by-product of the leather industry. The present study on ball-milled bovine type I collagen examined the documented cross-linking capabilities of glutaraldehyde and dehydrothermal drying with the relatively new enzymatic cross-linking technique involving microbial transglutaminase. To assess the degree of cross-linking by each technique, free amine residues remaining after cross-linking, collagenase resistance and size of cross-linked complexes were determined. Glutaraldehyde cross-linking resulted in the least number of free amines, highest molecular weight aggregates and highest resistance to collagenase degradation. Dehydrothermal drying also produced high molecular weight aggregates, but partially hydrolyzed the protein, making the fibril more susceptible to collagenase. Microbial transglutaminase treated collagen produced large molecular weight aggregates and was more resistant to collagenase degradation than control collagen. This new cross-linking technique warrants additional research attention. En ligne : https://drive.google.com/file/d/1D7vQjt_L_mlKI7riEvxjPUN5GY86B99K/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4067
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. C, N° 5 (05/2005) . - p. 196-202[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 002056 - Périodique Bibliothèque principale Documentaires Disponible Method to extract water-soluble collagen from induced biphasic commercial gel / Matthew J. Mastauskas in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVII, N° 7 (07/2012)
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Titre : Method to extract water-soluble collagen from induced biphasic commercial gel Type de document : texte imprimé Auteurs : Matthew J. Mastauskas, Auteur ; Gennaro J. Maffia, Auteur Année de publication : 2012 Article en page(s) : p. 243-248 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Collagène -- Solubilité
Eau
Extraction (chimie)
Gel de collagèneIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Water-soluble collagen extracted from commercial collagen gel could be a possible replacement for water-insoluble collagen fibrils, which are currently extracted from raw corium. If the water-soluble collagen proves to be a suitable replacement in the various water-insoluble collagen applications as mention in this paper, then the time-intensive milling process could be avoided. The first part of the process as described in this paper is a method to extract the water-soluble collagen. Water-soluble collagen was extracted from commercial collagen gel by mixing distilled water with the collagen gel, centrifugation, decanting, freezing and vacuum drying the supernate. Various ratios of commercial collagen gel to water ranging from 10% to 90% commercial collagen gel to water were examined based upon the extraction and performance of gravimetric analyses on the water-soluble collagen. The commercial collagen gel to water ratio had an effect on the mass fraction of extracted water-soluble collagen. Greater amounts of water-soluble collagen could be extracted by using lesser amounts of commercial collagen gel. The water-soluble collagen matrices had a mesh-like appearance similar to cotton, except that they could be flattened easily and could not retain their original shape. The water-soluble collagen matrices were formed into a chaotic, non-uniform manner caused by the re-constituting of fibers during the freezing and vacuum drying process. Note de contenu : - INTRODUCTION : Introduction to collagen - Water-soluble collagen
- EXPERIMENTAL : Experimental overview - Materials - Centrifugation study - Extraction process
- RESULTS AND DISCUSSION : Collagen composition of commercial collagen gel - Mass fraction of water-soluble collagen matrices - Microscopy of commercial collagen gel - Microscopy of water-soluble collagen matrix - SEM - waterxoluble collagen matrix
- CONCLUSIONS : Collagen composition of commercial collagen gel - Mass fraction of water-soluble collagen matrices - Microscopy of commercial collagen gel - Microscopy of water-soluble collagen matrices - SEM - water-soluble collagen matricesEn ligne : https://drive.google.com/file/d/1FwN0_eWMG-lD3IVo86Y7ubbXTn2Wvcz4/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=15644
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CVII, N° 7 (07/2012) . - p. 243-248[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 14063 - Périodique Bibliothèque principale Documentaires Disponible Recent advances in collagen based technologies / Gennaro J. Maffia in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 2 (02/2002)
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Titre : Recent advances in collagen based technologies Type de document : texte imprimé Auteurs : Gennaro J. Maffia, Auteur ; Maria Slomiana, Auteur ; John F. Davis Année de publication : 2002 Article en page(s) : p. 74-82 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Collagen dispersions, produced from ground bovine corium, have a remarkable water retention capability. This property has lead to research on applications in environmental remediation, biotechnology, biomedical engineering, and materials of construction. Widener researchers and collaborators are studying specific applications in all of these areas. Within the past year, research has focused on three areas: dispersion rheology, weighted and magnetic matrices (especially microspheres), and building materials. Initial results are promising in each of these focus areas, although the production technology remains long and labor intensive. Collagen dispersions take a minimum of two weeks to prepare and crosslinked matrices can take as long as two months. Future research is ongoing to further develop the potential applications and to scale-up and shorten the production process. En ligne : https://drive.google.com/file/d/1LPDpJld7BR9EZ8K-E4bYOuntTcTYW5UU/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4326
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Code-barres Cote Support Localisation Section Disponibilité 001571 - Périodique Bibliothèque principale Documentaires Disponible The effect of ultrasound on bovine hide collagen structure / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CI, N° 7 (07/2006)
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Titre : The effect of ultrasound on bovine hide collagen structure Type de document : texte imprimé Auteurs : Eleanor M. Brown, Auteur ; Donna M. Stauffer, Auteur ; Peter H. Cooke, Auteur ; Gennaro J. Maffia, Auteur Année de publication : 2006 Article en page(s) : p. 274-283 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Applications of ultrasound in leather processing have been researched for more than 50 years. Although these studies showed that ultrasound could have beneficial effects on hide preparation, tanning and finishing processes, the costs associated with the development of a new technology outweighed the benefits. Ultrasound is now a mature science, used to improve the efficiency of processes for the manufacture of a variety of materials. It may well offer a path toward the use of fewer (less) chemicals in the production of quality leather. However, the effects of ultrasound on the structure and function of biomacromolecules, specifically protein complexes, have not been extensively studied. This research examines the chemical, physical and mechanical effects of ultrasonic treatment on bovine hide collagen. Scanning electron micrographs show that low frequency, high power ultrasound (20 kHz) appears to unravel the 50 - 100 nm fibrils, seen in ball-milled collagen, into smaller diameter fibrils. Although these smaller fibrils are more susceptible to attack by collagenase, the individual collagen molecules remain intact as demonstrated by SDS-PAGE. Soluble and insoluble collagen and hide powder are also being examined to develop a broader picture of potential effects of ultrasound in leather manufacturing. En ligne : https://drive.google.com/file/d/13jfj1yMy-YFy1efthCdOrWWv0YvbSE_U/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=3997
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Code-barres Cote Support Localisation Section Disponibilité 005100 - Périodique Bibliothèque principale Documentaires Disponible