A model for proteolytic depliation of skins / D. Brady in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXV (Année 1990)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXXXV (Année 1990) . - p. 334-343 Titre : A model for proteolytic depliation of skins Type de document : texte imprimé Auteurs : D. Brady, Auteur ; J. R. Duncan, Auteur ; Alan E. Russell, Auteur Année de publication : 1990 Article en page(s) : p. 334-343 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : Research involving selected combinations of commercial proteases provided evidence that a synergistic depilatory effect occurs when proteases of complementary bond specificities are used in conjunction in enzymic depilatory preparations. Some form of strong alkali treatment of skins was found to be necessary to produce a skin fibre matrix of the prerequisite quality when the skin was depilated by proteases since, otherwise, the depilated skin after acetone dehydration was found to be depleted and stiff. Calcium hydroxide alone was found to be inadequate for this task, probably owning to the fact that it is less alkaline than the lime-sulfide mixture. Sodium hydroxide was therefore used in conjunction with calcium hydroxide (lime) to match the alkalinity of the lime-sulfide solution in order to produce skin characteristics comparable with those from a line-sulfide unhairing treatment. A combinaison of the information provided by the results obtained in the present systematic study combined with information gleaned from the relevant literature allowed for the construction of a model to represent the possible mechanism of enzymic depilation of skins. In terms of this model, depilation is caused by the disruption of the basement membrane at the dermal-epidermal junction through the degradation of its constituent molecular components by combinations of proteases with completely specifities, resulting in the removal of both the epidermis and associated wool or hair. En ligne : https://drive.google.com/file/d/1qy3G63b_brAZRW5U54vDu0o3VRg3F6Ox/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8724 [article]

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Partial purification of an extracellular protease produced by proteus vulgaris / D. Brady in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 78, N° 5 (09-10/1994)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 78, N° 5 (09-10/1994) . - p. 153-156 Titre : Partial purification of an extracellular protease produced by proteus vulgaris Type de document : texte imprimé Auteurs : D. Brady, Auteur ; J. R. Duncan, Auteur ; Alan E. Russell, Auteur Année de publication : 1994 Article en page(s) : p. 153-156 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : The proteolytic activity produced by a strain of Proteus vulgaris isolated in this laboratory from a stalling hide exhibiting depilation was studied. The Proteus vulgaris bacterium apparently produced a single protease or protease complex according to ion exchange and gel exclusion chromatography. The protease had maximal proteolytic activity in the 8.0-9.0 pH unit rage and was quite stable at high salinities (1.0 M). The protease was heat labile being increasingly inactivated when exposed to temperatures above 30°C ; the inclusion of divalent calcium ions failed to significantly thermostabilise the protease. The protease had a molecular mass of 44 000 daltons. En ligne : https://drive.google.com/file/d/1BSNnQbyfU6d0HEweukJ8lpP6rMG7FCIU/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8266 [article]

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