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675 : Technologie du cuir et de la fourrure |
Ouvrages de la bibliothèque en indexation 675
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Heterogeneous interaction between sulpho-syntans and collagen, part 6 / Z. Korenek in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 3 (05-06/1992)
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Titre : Heterogeneous interaction between sulpho-syntans and collagen, part 6 : Influence of reaction conditions and sulpho-syntan oligoelectrolyte molecular parameters Type de document : texte imprimé Auteurs : Z. Korenek, Auteur ; M. Vondruska, Auteur ; J. Mikulik, Auteur ; Z. Vinklà rek, Auteur Année de publication : 1992 Article en page(s) : p. 75-82 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Recently described PELC stoichiometry has been verified for the reaction between collagen fibres (BAT) and oligoelectrolytes (OEL) and its dependence on reaction conditions, structural and molecular parameters of OEL. It has been found that within a certain region of reaction conditions there occurs a stabilization of the chemical composition of the resultant compound for each of the OEL studied which correspond to stoichiometric polyelectrolyte complex of the pendent-pendent type. As has been shown by measuring the shrinkage temperature of tanned BAT samples their hydrothermal stability rises with the increasing level of irreversibly bound OEL up to the point of formation of a stoichiometric PELC ; hydrothermal stability does not change further with increases in bound OEL above this point (stoichiometry). Further, it has been found that, unlike stoichiometry, hydrothermal stability is significantly dependent on the structural and molecular parameters of the OEL. En ligne : https://drive.google.com/file/d/1jfYGfGk3FUNQ-qTmjjnrrrbLaLk0cPCh/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8609
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 76, N° 3 (05-06/1992) . - p. 75-82[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 006986 - Périodique Bibliothèque principale Documentaires Disponible Heterogeneous interaction between sulpho-syntans and collagen, part 7 / Z. Vinklà rek in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 76, N° 5 (09-10/1992)
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Titre : Heterogeneous interaction between sulpho-syntans and collagen, part 7 : Polyionic network hypothesis Type de document : texte imprimé Auteurs : Z. Vinklà rek, Auteur ; Z. Korenek, Auteur ; J. Vaculik ; M. Vondruska Année de publication : 1992 Article en page(s) : p. 162-168 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : During the reaction between oligoelectrolyte and collagen, a polyelectrolyte complex of the pendent-pendent type is formed. This kind of intermolecular complex has the structure of a three dimensional polyionic network, which is only intrafibrilliary polyionic network has been discussed theoretically. The structure of collagen compounds with oligoelectrolyte on the basis of naphthalene-2-sulphonic acid condensed with formaldehyde (syntanin) has then been followed up experimentally by scanning electron microscopy (SEM) and its correspondence to theroretical assumptions has been discussed. En ligne : https://drive.google.com/file/d/11vNW7j0gitPbjrCzqBRA317n0_AL5nVx/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8575
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Code-barres Cote Support Localisation Section Disponibilité 006988 - Périodique Bibliothèque principale Documentaires Disponible Heterogeneous interaction between sulpho-syntans and collagen. Part I : qualitative approach / Z. Vinklà rek in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 72 (Année 1988)
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Titre : Heterogeneous interaction between sulpho-syntans and collagen. Part I : qualitative approach Type de document : texte imprimé Auteurs : Z. Vinklà rek, Auteur ; M. Vondruska, Auteur ; J. Kupec, Auteur Année de publication : 1988 Article en page(s) : p. 177-182 Note générale : Bibliogr. Langues : Anglais (eng) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Interaction between sulpho-syntans and collagen represents a specific case of interation between two oppositely charged polyelectrolytes (PEL) resulting in polyelectrolyte complex formation. The specificity of this interaction relates to the fact that collagen (a polyampholyte having a spatially arranged structure of its own) must be converted into a polycation by means of protonisation and also that the whole process is complicated by heterogeneous conditions. In spite of this specificity, the interaction must conform to the general rules of formation of polyelectrolyte complexes for which electrostatic Coulomb's forces control combination in the initial phase. En ligne : https://drive.google.com/file/d/1CswgNLB1S3ewV4A1q6W174X1MoIxkt_4/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=9110
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Code-barres Cote Support Localisation Section Disponibilité 007134 - Périodique Bibliothèque principale Documentaires Disponible Heterologous expression of alkaline metalloproteinases in bacillus subtilis sck6 for eco-friendly enzymatic unhairing of goatskins / Shihao Zhang in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVII, N° 3 (03/2022)
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Titre : Heterologous expression of alkaline metalloproteinases in bacillus subtilis sck6 for eco-friendly enzymatic unhairing of goatskins Type de document : texte imprimé Auteurs : Shihao Zhang, Auteur ; Ruoshi Zhang, Auteur ; Xiaoguang Li, Auteur ; Zhe Xu, Auteur ; Yongqiang Tian, Auteur Année de publication : 2022 Article en page(s) : p. 113-123 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Caractérisation
Cuirs et peaux -- Propriétés mécaniques
Cuirs et peaux de chèvres
Epilage enzymatique
Matériaux -- Coloration
Métalloprotéinases
Wet-blue (tannage)Peau tannée au chrome (le chrome donne une couleur bleue)Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : In this study, alkaline metalloprotease gene 1067 was cloned from Planococcus halotolerans SCU63T and heterologously expressed in Bacillus subtilis SCK6. Using Luria Bertani (LB) broth medium as the initial medium, the optimal medium was obtained through a series of fermentation and culture optimization (g/L): yeast extract (10), soybean powder (15), urea (20), potassium chloride (6.7), calcium chloride (13.3), NaCl (10). On the basis of the optimal medium, the highest enzymatic activity of 1259.21 U/mL could be obtained by culturing at 30°C for 40 h. with pH 8, inoculation amount of 4% and filling amount of 50 mL. EDTA inhibits protease activity and PMSF promotes it, indicating that it was a metalloprotease rather than a serine protease. The optimum reaction temperature of the protease is 70°C, and the optimum pH is 9. The metal ions Zn 2+, Co2+ and surfactant β-ME, Tween 80 can improve the activity of the protease. The results of unhairing, SEM and staining show that this metalloprotease can completely dehair goatskin. Compared with the conventional chemical method, the goatskin after enzymatic unhairing has softer texture and smoother surface, and there is no obvious damage to the goatskin. Note de contenu : - MATERIALS AND METHODS : Materials - Construction of recombinant plasmid and expression of 1067 in B. subtilis SCK6 - Optimization of fermentations conditions - Purification of protease 1067 - Enzyme assay - Analysis of enzymatic properties - Unhairing function of protease 1067 - Characterization of protease 1067 unhairing
- RESULTS AND DISCUSSION : Construction of recombinant strain and identification of protease activity - Fermentation optimization - Purification and identification of protease 1067 - Effect of temperature on enzyme activity and stability - Effect of pH on enzyme activity and stability - Effect of metal ions on enzyme activity - Effects of chemicals on enzyme activity - Effect of organic solvents on enzyme activity - Analysis of unhairing - SEM and analysis of tissue staining
- Table 1 : Factors and levels for RSM
- Table 2 : ANOVA for quadratic model
- Table 3 : Effect of metal ions on enzyme activity
- Table 4 : Effect of chemicals on enzyme activity
- Table 5 : Effect of solvents on enzyme activity
- table 6 : Characterization of mechanical properties of wet blue skinDOI : https://doi.org/10.34314/jalca.v117i3.4892 En ligne : https://drive.google.com/file/d/1z4VjDZxnKDTJf0c5BtRxJKAwUieQ2jK9/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37602
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CXVII, N° 3 (03/2022) . - p. 113-123[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 23402 - Périodique Bibliothèque principale Documentaires Disponible Heterologous expression of metalloproteinases from planococcus halotolerans SCU63T and eco-friendly enzymatic dehairing of goatskin / Zhang Shihao in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 105, N° 3 (05-06/2021)
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Titre : Heterologous expression of metalloproteinases from planococcus halotolerans SCU63T and eco-friendly enzymatic dehairing of goatskin Type de document : texte imprimé Auteurs : Zhang Shihao, Auteur ; Ruoshi Zhang, Auteur ; Xiaoguang Li, Auteur ; Zhe Xu, Auteur ; Yongqiang Tian, Auteur Année de publication : 2021 Article en page(s) : p. 132-139 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Caractérisation
Cuirs et peaux de chèvres
Enzymes microbiennes
Epilage enzymatique
Métalloprotéinases
Microscopie électronique à balayage
Peptidases
pH
Produits chimiques -- Purification
Travail de rivière (cuir)Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : In this study, a metalloproteinase gene from Planococcus halotolerans SCU63 was cloned and expressed in Bacillus sp. SCK6. LB broth medium was used as the initial medium and for a series of fermentation optimisations. The most suitable medium components were as follows (g/l) : yeast extract powder (20), casein (13), tryptone (7), NaCl (10), urea (8). When the inoculation amount was 2%, the filling amount was 100mL, the culture time was 370C, and the pH was 7.0 for 40 hours the protease production reached the highest. The enzyme activity was completely inhibited by EDTA. Surfactants, such as Tween 20, Tween 80, and TritonX-100, could improve the enzyme activity, while SDS could inhibit the enzyme activity. Under protease action, goatskin can be completely depilated at 37oc and 28 hours. Compared with the conventional chemical dehairing, the enzymatic dehairing opened up the goatskin elastic fibre without any hair root in the hair follicle, and the skin was of high quality. Note de contenu : - MATERIALS AND METHODS : Materials - Construction of recombinant plasmid and expression of 1030 in B. subtilis SCK6 - Optimisation of fermentation conditions - Purification of proteases - Determination of enzyme activity - Characterisation of enzymatic properties - Dehairing function of protease 1030 - Analysis of dehairing
- RESULTS : Construction of recombinant plasmid and its expression in SCK6 - Optimisation of fermentation conditions and RSM - Purification and identification of proteases 1030 - Effect of temperature on enzyme activity and stability - Effect of pH on enzyme activity and stability - Effect of NaCl concentration on enzyme activity - Effect of metal ions on enzyme activity - Effect of chemicals on enzyme activity - Effect of organic solvents on enzyme activity - Analysis of enzymatic dehairing - Analysis of SEM and staining
- Table 1 : Factors and levels for RSM
- Table 2 : ANOVA for quadratic model
- Table 3 : Effect of metal ions on enzyme activity
- Table 4 : Effect of chemicals on enzyme activity
- Table 5 : Effect of solvents on enzyme activityEn ligne : https://drive.google.com/file/d/15BWASUeWYefKBb5gBjgfaEyNcAG7bjbz/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=35833
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Code-barres Cote Support Localisation Section Disponibilité 22745 - Périodique Bibliothèque principale Documentaires Disponible Hide and leather characteristics of afrikaner and friesland bulls and steers slaughtered at various ages between birth and 24 months / Alan E. Russell in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 61 et 62 (Années 1977 et 1978)
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PermalinkHide and leather characteristics of afrikaner and friesland bulls and steers slaughtered at various ages between birth and 24 months / Alan E. Russell in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 61, N° 1 (01-02/1977)
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PermalinkHide and leather characteristics of young afrikaner-type steers slaughtered at four different live masses / Alan E. Russell in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 64, N° 1 (01-02/1980)
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PermalinkHide and skin - What's in it for you ? / Amanda Michel in LEATHER INTERNATIONAL, Vol. 210, N° 4789 (04/2009)
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PermalinkHide and skins : physical change and effects within chemical processing / Richard Daniels in WORLD LEATHER, Vol. 18, N° 5 (08/2005)
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PermalinkHide collagen as a food / R. L. Henrickson in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXV (Année 1980)
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PermalinkHide defects of feedlot cattle : Assessment of cattle management, breed type, sex, live market weight, and source factors on hide quality / W. T. Wright in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVI, N° 4 (04/2021)
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PermalinkHide powder azure and azocoll as substrates for assay of the proteolytic activity of bate / Samuel M. Mozersky in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXVII, N° 8 (08/1992)
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PermalinkHide protein as a food additive / R. L. Henrickson in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXIX (Année 1984)
PermalinkHide, skin and leather defects : a guide to their microscopy / Mary Dempsey / Palmerston North [Nouvelle Zélande] : New Zealand Leather and Shoe Research Association (1984)
PermalinkPermalinkHides and skins / Education Committee National Hide Association / Sioux City [Etats-Unis] : National Hide Association (1979)
PermalinkHides and skins : temperature and physical change / Richard Daniels in WORLD LEATHER, Vol. 18, N° 5 (08/2005)
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PermalinkHides, skins and leather under the microscope / The British Leather Manufacturers'Research Association / Egham [United Kingdom] : The British Leather Manufacturers'Research Association (1956)
PermalinkHigh-efficiency bio-degreasing technology for leather making - Characterization of catalytic hydrolysis properties of lipases towards fats based on greasy skin powder substrate / Yongkang Luo in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXIV, N° 11 (11/2019)
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PermalinkHigh exhaust acrylic chemistry / Anton El A'mma in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVIII, N° 1 (01/2003)
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PermalinkHigh performance acrylic polymer technology for use in leather finishing processes / J. Hoefler in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 8 (08/2013)
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PermalinkHigh performance acrylic resins / J. J. Biles in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXIX (Année 1984)
PermalinkHigh performance acrylic resins for leather - 2 acrylic topcoating systems / J. J. Biles in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXII (Année 1987)
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PermalinkHigh performance finishing with water-borne transfer systems - Technical note / J. Levy in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXIX, N° 3 (03/1994)
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