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dc.creatorQiu, Jingwen
dc.creatorWilkens, Casper
dc.creatorBarrett, Kristian
dc.creatorMeyer, Anne S.
dc.date.accessioned2020-08-18T20:47:05Z
dc.date.available2020-08-18T20:47:05Z
dc.date.created2020
dc.identifier.issn0734-9750spa
dc.identifier.otherhttps://doi.org/10.1016/j.biotechadv.2020.107607spa
dc.identifier.urihttp://hdl.handle.net/20.500.12010/11942
dc.description.abstractKeratin is an insoluble and protein-rich epidermal material found in e.g. feather, wool, hair. It is produced in substantial amounts as co-product from poultry processing plants and pig slaughterhouses. Keratin is packed by disulfide bonds and hydrogen bonds. Based on the secondary structure, keratin can be classified into α-keratin and β-keratin. Keratinases (EC 3.4.-.- peptide hydrolases) have major potential to degrade keratin for sustainable recycling of the protein and amino acids. Currently, the known keratinolytic enzymes belong to at least 14 different protease families: S1, S8, S9, S10, S16, M3, M4, M14, M16, M28, M32, M36, M38, M55 (MEROPS database). The various keratinolytic enzymes act via endo-attack (proteases in families S1, S8, S16, M4, M16, M36), exo-attack (proteases in families S9, S10, M14, M28, M38, M55) or by action only on oligopeptides (proteases in families M3, M32), respectively. Other enzymes, particularly disulfide reductases, also play a key role in keratin degradation as they catalyze the breakage of disulfide bonds for better keratinase catalysis. This review aims to contribute an overview of keratin biomass as an enzyme substrate and a systematic analysis of currently sequenced keratinolytic enzymes and their classification and reaction mechanisms. We also summarize and discuss keratinase assays, available keratinase structures and finally examine the available data on uses of keratinases in practical biorefinery protein upcycling applicationsspa
dc.format.extent45 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.publisherBiotechnology Advancesspa
dc.sourcereponame:Expeditio Repositorio Institucional UJTLspa
dc.sourceinstname:Universidad de Bogotá Jorge Tadeo Lozanospa
dc.subjectα-keratinspa
dc.subjectβ-keratinspa
dc.subjectKeratinasesspa
dc.subjectKeratinase assayspa
dc.subjectKeratinase classificationspa
dc.subjectKeratinolytic mechanismsspa
dc.subjectKeratinase crystal structuresspa
dc.subjectBiocatalysisspa
dc.subjectProtein recyclinspa
dc.titleMicrobial enzymes catalyzing keratin degradation: Classification, structure, functionspa
dc.type.localArtículospa
dc.subject.lembSíndrome respiratorio agudo gravespa
dc.subject.lembCOVID-19spa
dc.subject.lembSARS-CoV-2spa
dc.subject.lembCoronavirusspa
dc.rights.accessrightsinfo:eu-repo/semantics/embargoedAccessspa
dc.type.hasversioninfo:eu-repo/semantics/acceptedVersionspa
dc.rights.localAcceso restringidospa
dc.identifier.doihttps://doi.org/10.1016/j.biotechadv.2020.107607spa


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