Optimization of keratinolytic protease production by purpureocillium lilacinum LPS # 876 as a sustainable management of tannery hair waste / Ivana Alejandra Cavello in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 8 (08/2013)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CVIII, N° 8 (08/2013) . - p. 300-310 Titre : Optimization of keratinolytic protease production by purpureocillium lilacinum LPS # 876 as a sustainable management of tannery hair waste Type de document : texte imprimé Auteurs : Ivana Alejandra Cavello, Auteur ; Sebastiàn Fernando Cavalitto, Auteur Année de publication : 2013 Article en page(s) : p. 300-310 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Biodégradation Cuirs et peaux -- Déchets -- Recyclage Déchets organiques -- Recyclage Kératinases Poils -- Recyclage Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : Hair waste is recognized as a solid waste generated after a hair-saving unhairing process in leather technology, and it is produced in large amounts in Buenos Aires province, Argentine. The present method for this solid waste is disposal, which is environmentally troublesome and costly for the tanneries. Biodegradation of hair waste by keratinolytic microorganisms represents an alternative for bioconversion of keratin waste. This paper reports the optimization of keratinases production by Purpureocillium lilacinum LPS # 876. Firstly, one factor-at-a-time method was used to investigate the effect of nitrogen-sources, metal ions concentration in the basal mineral medium, as well as, initial pH and temperature on enzyme production. Medium composition for the keratinases production by P. lilacinum was optimized using two statistical methods: Plackett-Burman design and central composite design -combined with response surface methodology- used to optimize three significant variables: initial pH, glucose and CaCl2. The optimal conditions were determined as 7.10 g l-1 of glucose; 0.0065 mg l-1 of CaCl2 and initial pH of 5.60; at this condition the maximum keratinase yield predicted was 26.7 U ml-1. The model validation showed that it described adequately the influence of glucose and calcium concentration and initial pH on enzyme production. Production of keratinases by P. lilacinum is a less-exploited field that might represent a novel and promising biotechnological application for this microorganism. Note de contenu : - MATERIALS AND METHODS : Reagents - Microorganism and culture conditions - Determination of proteolytic activity - OPTIMIZATION OF FERMENTATION MEDIUM USING ONE-VARIABLE-AT-A-TIME METHOD : Effect of environmental conditions on production keratinases - Effect of the concentration of the metal ions present in the basal mineral medium - Effect of the addition of some salts on keratinolytic enzymes production - Effect of nitrogen sources - Identification of the significant factors by Plackett-Burman (PB) design - Central Composite Design and Response Surface Methodology - BIOCHEMICAL PROPERTIES OF CRUD ENZYME : Detection of keratinolytic activity on polyacrylamide gels (casein and keratin-zymograms) - Substrate specificity - RESULTS : Optimization using one-variable-at-a-time approach - Selection of significant variables by Plackett-Burman design - Optimization by response surface methodology (RSM) - Detection of keratinolytic activity on polyacrylamide gels (casein and keratin-zymograms) - Substrate specificity En ligne : https://drive.google.com/file/d/1UOY6o8dh6sX7U4bHC-G1WlIdxLmn3DgC/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=19179 [article]

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