dc.creatorMazotto, Ana Maria
dc.creatorde Melo, Ana Cristina N. de
dc.creatorMacrae, Andrew
dc.creatorRosado, Alexandre Soares
dc.creatorPeixoto, Raquel
dc.creatorCedrola, Sabrina M. L.
dc.creatorCouri, Sônia
dc.creatorZingali, Russolina B.
dc.creatorVilla, Ana Lúcia V.
dc.creatorRabinovitch, Leon
dc.creatorChaves, Jeane Q.
dc.creatorVermelho, Alane B.
dc.date2019-05-28T11:03:32Z
dc.date2019-05-28T11:03:32Z
dc.date2011
dc.date.accessioned2023-09-26T21:50:39Z
dc.date.available2023-09-26T21:50:39Z
dc.identifierMAZOTTO, Ana Maria et al. Biodegradation of feather waste by extracellular keratinases and gelatinases from Bacillus spp. World J Microbiol Biotechnol., v. 27, p.1355–1365, 2011.
dc.identifier0959-3993
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/33240
dc.identifier10.1007/s11274-010-0586-1
dc.identifier1573-0972
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8873786
dc.descriptionIn this study, three feather degrading bacterial strains were isolated from agroindustrial residues from a Brazilian poultry farm. Three Gram-positive, spore-forming, rod-shaped bacteria and were identified as B. subtilis 1271, B. licheniformis 1269 and B. cereus 1268 using biochemical, physiologic and molecular methods. These Bacillus spp. strains grew and produced keratinases and peptidases using chicken feather as the sole source of nitrogen and carbon. B. subtilis 1271 degraded feathers completely after 7 days at room temperature and produced the highest levels of keratinase (446 U ml(-1)). Feather hydrolysis resulted in the production of serine, glycine, glutamic acid, valine and leucine as the major amino acids. Enzymography and zymography analyses demonstrated that enzymatic extracts from the Bacillus spp. effectively degraded keratin and gelatin substrates as well as, casein, hemoglobin and bovine serum albumin. Zymography showed that B. subtilis 1271 and B. licheniformis 1269 produced peptidases and keratinases in the 15-140 kDa range, and B. cereus produced a keratinase of ~200 kDa using feathers as the carbon and nitrogen source in culture medium. All peptidases and keratinases observed were inhibited by the serine specific peptidase inhibitor phenylmethylsulfonyl fluoride (PMSF). The optimum assay conditions of temperature and pH for keratinase activity were 40-50°C and pH 10.0 for all strains. For gelatinases the best temperature and pH ranges were 50-70°C and pH 7.0-11. These isolates have potential for the biodegradation of feather wastes and production of proteolytic enzymes using feather as a cheap and eco-friendly substrate.
dc.description2022-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherSpringer
dc.rightsrestricted access
dc.subjectBacillus spp.
dc.subjectPeptidase
dc.subjectQueratinase
dc.subjectQueratina de penas
dc.subjectDegradação de penas
dc.subjectBacillus spp.
dc.subjectFeather degradation
dc.subjectFeather keratin
dc.subjectKeratinase
dc.subjectPeptidase
dc.titleBiodegradation of feather waste by extracellular keratinases and gelatinases from Bacillus spp
dc.typeArticle


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