[article]
Titre : |
A novel approach for quantitative characterization of hydrolytic action of glycosidases to glycoconjugates in leather manufacturing |
Type de document : |
texte imprimé |
Auteurs : |
Fengxiang Luo, Auteur ; Zhong Xiang, Auteur ; Chunxiao Zhang, Auteur ; Biyu Peng, Auteur ; Zhongzhen Long, Auteur |
Année de publication : |
2020 |
Article en page(s) : |
p. 263-269 |
Note générale : |
Bibliogr. |
Langues : |
Américain (ame) |
Catégories : |
Caractérisation Epilage enzymatique Essais (technologie) Glycoprotéines GlycosidasesLes Glycoside hydrolases (ou glycosidases) catalysent l'hydrolyse de liaisons glycosidiques et libèrent au moins un composé osidique. Ce sont des enzymes extrêmement communes, dont les rôles sont aussi divers que la dégradation des glucides complexes (cellulose et hémicellulose), les défenses anti-bactériennes (ex. le lysozyme), la pathogénicité (ex. les neuraminidases virales) ou le métabolisme cellulaire (amylases ou enzyme de débranchement du glycogène pour le métabolisme énergétique, mannosidases comme modulateur de glycosylation des protéines, ...). Les glycosyltransférases et les glycosides hydrolases sont les deux classes majeures d'enzymes impliquées dans la synthèse et la rupture des liaisons osidiques. Hydrolyse enzymatique Peaux brutes -- Trempe Poudre de peaux
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Index. décimale : |
675 Technologie du cuir et de la fourrure |
Résumé : |
Glycoconjugates, herein glyco-protein conjugates, composed of protein and saccharide chains are the main components of the interfibrillar matrix in skin which need to be fully removed in the leather making process. The application of glycosidases can assist unhairing and skin fiber opening-up, resulting in the improvement of leather quality, by breaking the glycoconjugates safely and efficiently in mild conditions. The biotechnology assisted by glycosidases, a big family of over 200 kinds of enzymes, has a great potential but the related mechanisms and the efficiency of different glycosidases are still not clear, which interferes with its wide application. To screen the proper glycosidases, a novel method of evaluating the catalytic hydrolysis properties of glycosidases towards skin glycoconjugates based a special hide powder substrate, simulating the actual leather processing, was established through detecting the produced amount of the total sugar in the solution. The special substrate was prepared, the determination conditions were optimized, then the performances of several typical glycosidases were evaluated and their application effects in soaking process of leather making were also investigated. The results show that the optimum testing conditions are lower than 4 h of the reacting time, optimally 2 h, and lower than 40 U/mL of the enzyme concentration, optimally 0-25 U/mL based on 2 g of the substrate; the results to evaluate the properties of some glycosidases based on the established method are positively related to their applying effects in soaking. The new method with better repeatability can be used as an available tool to correctly select glycosidases and optimize process parameters for correct use. |
Note de contenu : |
- MATERIALS AND METHODS : Materials - Preparation of the hide powder substrate containing glycoconjugates - Assay of glycosidase activity based on the prepared substrate - Optimization of parameters of the testing method - Glycosidase soaking trial
- RESULTS AND DISCUSSION : Parameters of the prepared hide powder substrate - Optimization of the testing conditions in detecting glycosidase activity - Evaluation of properties of typical glycosidases - Relationship between glycosidases activities to glycoconjugates and soaking effect |
DOI : |
https://doi.org/10.34314/jalca.v115i7.3836 |
En ligne : |
https://drive.google.com/file/d/1kbuXsp8wOESPhNaKvy8ct9TgkMOnJu9y/view?usp=drive [...] |
Format de la ressource électronique : |
Pdf |
Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=34328 |
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CXV, N° 7 (07/2020) . - p. 263-269
[article]
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