Collagen recovered, purified and enzymatically hydrolysed from tannery waste / M. E. Errasti in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 108, N° 1 (01-02/2024)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 108, N° 1 (01-02/2024) . - p. 1-8 Titre : Collagen recovered, purified and enzymatically hydrolysed from tannery waste Type de document : texte imprimé Auteurs : M. E. Errasti, Auteur ; Laura M. I. Lopez, Auteur Année de publication : 2024 Article en page(s) : p. 1-8 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène Cuirs et peaux -- Déchets -- Recyclage Déchets industriels -- Recyclage Enzymes végétales Hydrolysat de collagène Hydrolyse Peptidases Produits chimiques -- Purification Récupération (Déchets, etc.) Tannage -- Déchets Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : One of the main challenges of the tannery industry is the management of the waste generated during the leather manufacturing process. This study aimed to recover the collagen from tanning industry waste to acquire knowledge about its conversion into high value-added ingredients with bio-functional properties. To this end, collagen was purified from rawhide waste from the leather industry, characterised by electrophoresis and compared with commercial collagen. Subsequently, it was subjected to an enzymatic treatment using plant proteases from Bromelia hieronymi under mild reaction conditions to produce hydrolysates, since the production of bioactive peptides by enzymatic hydrolysis is a sustainable way of taking advantage of protein by-products. The hydrolysates were characterised by matrix-assisted laser desorption/ionisation time-of-flight (MALDI TOF) mass spectrometry, showing peptides with molecular weights ranging from 1,000 to 6,000 Da. Liquid chromatography-mass spectrometry (LC-MS/MS) analysis allowed identifying 31 peptides from the a, chain of type I collagen and another 13 from the a2 chain of type I collagen. The probability that the peptides identified were bioactive was predicted with the Peptide Ranker software ('in silico analysis'). This demonstrated that 70% of them had high bioactive potential. These results showed that the collagen recovered from the waste of the tannery industry and hydrolysed by proteases from Bromelia hieronymi becomes a suitable source to obtain a product with greater added value than the original material and with multiple potential industrial applications. Note de contenu : - Chemicals - Collagen recovery - Plant enzymatic preparation - Preparation of collagen hydrolysate - Collagen hydrolysate characterisation - Table 1 : Chemical characterisation of the spiits before and alter the preliminary processing. Values are expressed as meant SD - Table 2 : HC peptides identified by LC-MS/MS and the potential to be bioactive (a Score obtained with PeptideRanker) En ligne : https://drive.google.com/file/d/1Y7TX9F5xRUSAxM8b0VRzEpEI3v406L0t/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=40927 [article]

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Fungal biotransformation of bovine hair : Part 1 - Isolation of fungus with keratinolytic activity / B. C. Galarza in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 88, N° 3 (05-06/2004)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 88, N° 3 (05-06/2004) . - p. 93-98 Titre : Fungal biotransformation of bovine hair : Part 1 - Isolation of fungus with keratinolytic activity Type de document : texte imprimé Auteurs : B. C. Galarza, Auteur ; L. M. Goya, Auteur ; Carlos S. Cantera, Auteur ; Maria Laura Garro, Auteur ; H. E. Reinos, Auteur ; Laura M. I. Lopez, Auteur Année de publication : 2004 Article en page(s) : p. 93-98 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Bovins Détérioration fongique Poils -- Biodégradation Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : The present study reports on the results of the “fungal biodegradation” of “hair waste” in a static solid medium using previously isolated strains of Trichophyton ajelloi and Fusarium oxysporum. The main purpose of the research programme is to upgrade the hair by biodegradation, to consider it as a raw material instead of the current modality of “throwing away” proteins to landfill and to its reuse in agricultural technology, directly or after composting and applying earthworms to generate an organic fertilizer (“vermicompost”). The fungal activity on the hair gives a degraded organic material and an extract with a pool of proteases with, amongst others, keratinolytic activity,. The enzyme activities expressed by the fungal extract are evaluated against soluble, insoluble, synthetic, and skin protein component substrates. Relationships between the different specific activities are defined to evaluate and predict the possible behaviour of the fungal extracts in the beamhouse processes. Note de contenu : - Solid state culture - Objectives - Experimental Development : Materials and Methods - Protocol of the analysis for activity assessment - Results and Discussion : Assessment of enzymatic activities of crude extracts - Aminopeptidase Activity. Determination of kinetic constants - Assessment of the degree of hair digestion - Protein profile and Isoelectric Focusing (IEF) - Zymogram - Comments on mechanisms of fungal digestion of hair - Fungal extracts in the soaking, unhairing and bating processes. Possible applications - Table 1 : Proteolytic activity of the fungal extracts of the different substrates - Table 2 : Activity Relationships for Trichophyton ajelloi and Fusarium oxysporum fungal extracts En ligne : https://drive.google.com/file/d/1Mrbx0x1BGf1ZNG_jsl1LMyTL1SX9KH-J/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=39634 [article]

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Hair saving unhairing process. Annex to part 5 (figures) - Characterisation of enzymatic preparations applied in soaking and unhairing processes / Carlos S. Cantera in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 87, N° 3 (05-06/2003)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 87, N° 3 (05-06/2003) . - p. 89-90 Titre : Hair saving unhairing process. Annex to part 5 (figures) - Characterisation of enzymatic preparations applied in soaking and unhairing processes Type de document : texte imprimé Auteurs : Carlos S. Cantera, Auteur ; L. Goya, Auteur ; Betina Galarza, Auteur ; Maria Laura Garro, Auteur ; Laura M. I. Lopez, Auteur Année de publication : 2003 Article en page(s) : p. 89-90 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Caractérisation Epilage enzymatique Index. décimale : 675 Technologie du cuir et de la fourrure Note de contenu : - Fig. 1 : Proteolytic activity as function of pH Enzymatic preparation : Alcamax Substrate: "Epidermis" - Fig. 2 : Proteolytic activity as function of pH Enzymatic preparation : Pellvit Substrate: "Epidermis" - Fig. 3 : Proteolytic activity as function of pH Enzymes: "Vegetal extract" Substrate : "Epidermis" - Fig. 4 : Proteolytic activity as function of pH Enzymatic preperations : Alcamax, Pellvit and "vegetal extract" Substrate: "Keratin Azure" - Fig. 5 : SDS-PAGE of Alcamax, Pellvit and "Vegetal extract" - Fig. 6 : Isoelectric focusing and zymogram of Alcamax, Pellvit and "Vegetal extract" En ligne : https://drive.google.com/file/d/1nXQCLGCpCO5EUfvslgNxDmtWRcNBqq5v/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=39780 [article]

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Hair saving unhairing process. Part 5 characterisation of enzymatic preparations applied in soaking and unhairing processes / Carlos S. Cantera in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 87, N° 2 (03-04/2003)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 87, N° 2 (03-04/2003) . - p. 69-77 Titre : Hair saving unhairing process. Part 5 characterisation of enzymatic preparations applied in soaking and unhairing processes Type de document : texte imprimé Auteurs : Carlos S. Cantera, Auteur ; L. Goya, Auteur ; Betina Galarza, Auteur ; Maria Laura Garro, Auteur ; Laura M. I. Lopez, Auteur Année de publication : 2003 Article en page(s) : p. 69-77 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Caractérisation Epilage enzymatique Peaux brutes -- Trempe Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Considering the importance that is attached to the characterisation of proteolytic enzymatic preparations employed in leather making, especially in the development of enzyme unhairing, our studies are aimed to develop a protocol of analysis that allows us to determine the behaviour of the enzymes on diverse protein skin substrates. In the protocol presented here it is important to highlight the incorporation of the so-called ‘epidermis substrate’, comprising the epidermis layer, hair and the root sheaths, as well as the procedure to assess enzymatic action on the proteoglycans. On two of the substrates, “epidermis” and Hide Powder Azure, studies on activation/inhibition of the enzyme activity using components usually added in the soaking and unhairing processes was also carried out. The protocol was applied to two commercial enzymatic preparations commonly used in leather processing, and to an extract of vegetable proteases that CITEC, jointly with LIPROVE, is applying in its investigation on enzyme unhairing. The protocol developed is a useful tool to assist us in the design of ideal enzyme unhairing: that in which the enzymatic activity is orientated towards the components of the epidermis system, when their action on fibrous proteins – particularly collagen - is minimised or avoided and when the leathers developed have the desired properties. Note de contenu : - INTRODUCTION : Chromogenic substrates - The epidermis layer, hair and root sheaths : the ‘epidermis substrate’ - Activity on proteoglycans (PGs) and hide powder substrate - OBJECTIVES - MATERIALS AND METHODS : 1) Assessment of protein content - 2) Assessment of activities on different substrates : Non – keratin based substrates - Activity upon proteoglycans (PGs). Hide powder substrate - Keratin-based substrates - 3) Inhibition and activation tests - 4) Protein Profile. Electrophoresis in SDS/polyacrylamide gel (PAGE) - 5) Isoelectric Focusing (IEF) - Zymogram - EXPERIMENTAL RESULTS - PROTEOLYTIC ACTIVITY AGAINST DIFFERENT SUBSTRATES AND ACTIVATION AND INHIBITION ASSAYS - ANALYSIS OF THE RESULTS : Activation and Inhibition Tests - Table 1 : Proteolytic activity of the enzymatic preparations against different substrates - Table 2 : Ranges of pH corresponding to 90% of the maximum activity for each one of the enzymatic preparations (maximum activity pH value is shown in brackets) - Table 3 : Changes in the activity of Alcamax and Pellvit against the chromogenic substrates hide powder azure and ‘epidermis’ adding components used in soaking and unhairing processes (*) En ligne : https://drive.google.com/file/d/1lrLmDHNIHN7pji0LbISFfwO_LGJtTNU1/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=39802 [article]

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Tannases and other fungal enzymes applicable to the transformation of tannins and their potential for bioremediation of effluents from the leather industry / Lorena V. Cortizo in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 106, N° 1 (01-02/2022)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 106, N° 1 (01-02/2022) . - p. 32-41 Titre : Tannases and other fungal enzymes applicable to the transformation of tannins and their potential for bioremediation of effluents from the leather industry Type de document : texte imprimé Auteurs : Lorena V. Cortizo, Auteur ; Laura M. I. Lopez, Auteur ; N. Saparrat, Auteur Année de publication : 2022 Article en page(s) : p. 32-41 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Bioremédiation Déchets industriels -- Elimination Eaux usées -- Epuration Enzymes fongiques Tanins Tannases Les tannases constituent une classe d'enzymes, de référence EC EC 3.1.1.20), qui catalysent les réactions chimiques : digallate + H2O ⇌ {\displaystyle \rightleftharpoons } \rightleftharpoons 2 gallate Les deux substrats de cette enzyme sont donc l'digallate et l'H2O, et son produit de réaction est le gallate. Cette enzyme appartient à la famille des hydrolases et plus spécifiquement à ceux qui agissent sur les liaisons ester carboxyliques. Le nom de cet classe d'enzyme est acylhydrolase tannique. Parmi les autres noms en vigueur, on trouve tannase S et acetylhydrolase tannique. En plus de catalyser l'hydrolyse de la liaison ester centrale entre les deux anneaux aromatiques du digallate (activité de dépsidase), les tannases peuvent aussi avoir une activité d'estérase (hydrolyse de la fonction ester terminale attachée à une des deux anneaux aromatiques). Les tannases sont des enzymes clé dans la dégradation des gallotanins, un type de tanins hydrolysables. On les trouve dans divers groupes de microorganisme, incluant les bactéries de la panse. Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : The use of fungal enzymes, such as tannases and oxidative enzymes, in the tannin bioconversion process offers great advantages over other biological and chemical technologies in terms of safety, re-use, and better control of process parameters, and is also a profitable and environmentally friendly method. Some reports have shown that different fungi can remove tannins from effluents, transforming them and/or detoxifying them, and using them, in some cases, as their only source of carbon. By means of different enzymes, these fungi trigger reactions that lead to the elimination of water-soluble tannins, which are the cause of toxicity in surface water bodies. Thus, these microorganisms are attractive to obtain enzyme cocktails applicable to the bioremediation of effluents rich in tannins, such as those derived from the leather industry. This review aims to provide updated information on fungal sources of enzymes able to transform tannins, with emphasis on tannases, and to show alternatives to culture tannase-producing fungi and obtain the enzymes and their activity in immobilization matrices. The inducible nature of the fungal synthesis of tannases reveals the importance of acquiring basic knowledge about the physiology of tannase-producing fungi and the need for studies in different culture and scaling systems. Note de contenu : - Tannins as targets of fungal enzymes - Potential of fungal enzymes to remove tannins : Tannases - Oxidative enzymes - Fungal tannase production methodologies : Solid-state fermentation (SSF) - Submerged fermentation (SMF) - Fungi and their activity in the removal and/or detoxification of tannins present ineffluents from the leather industry - Fig. 1 : Main mechanical structures of tannins - Fig. 2 : Possible mechanisms involved in tannin removal by fungi - Table 1 : Production of tannases from fungal culture systems under solid state-fermentation conditions (SSF) by using natural substrates - Table 2 : Fungal culture systems under submerged fermentation (SMF) for tannase production En ligne : https://drive.google.com/file/d/1n9kFXj5bJpWHkYr0JY6KpK4cgxxUU52m/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=36970 [article]

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