Purification and characterization of two xylanases from alkalophilic and thermophilic Bacillus licheniformis 77-2

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorDamiano, Valquiria B.-
Autor(es): dc.creatorWard, Richard-
Autor(es): dc.creatorGomes, Eleni-
Autor(es): dc.creatorAlves-Prado, Heloiza Ferreira-
Autor(es): dc.creatorDa Silva, Roberto-
Data de aceite: dc.date.accessioned2021-03-10T17:14:23Z-
Data de disponibilização: dc.date.available2021-03-10T17:14:23Z-
Data de envio: dc.date.issued2014-05-20-
Data de envio: dc.date.issued2014-05-20-
Data de envio: dc.date.issued2006-03-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1385/ABAB:129:1:289-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/19549-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/19549-
Descrição: dc.descriptionThe alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermostable cellulase-free xylanases. The crude xylanase was purified to apparent homogeneity by gel filtration (G-75) and ionic exchange chromatography (carboxymethyl sephadex, Q sepharose, and Mono Q), resulting in the isolation of two xylanases. The molecular masses of the enzymes were estimated to be 17 kDa (X-I) and 40 kDa (X-II), as determined by SDS-PAGE. The K(m) and V(max) values were 1.8 mg/mL and 7.05 U/mg protein (X-I), and 1.05 mg/mL and 9.1 U/mg protein (X-II). The xylanases demonstrated optimum activity at pH 7.0 and 8.0-10.0 for xylanase X-I and X-II, respectively, and, retained more than 75% of hydrolytic activity up to pH 11.0. The purified enzymes were most active at 70 and 75 degrees C for X-I and X-II, respectively, and, retained more than 90% of hydrolytic activity after 1 h of heating at 50 degrees C and 60 degrees C for X-I and X-II, respectively. The predominant products of xylan hydrolysates indicated that these enzymes were endoxylanases.-
Formato: dc.format289-302-
Idioma: dc.languageen-
Publicador: dc.publisherHumana Press Inc-
Relação: dc.relationApplied Biochemistry and Biotechnology-
Relação: dc.relation1.797-
Relação: dc.relation0,571-
Direitos: dc.rightsclosedAccess-
Palavras-chave: dc.subjectxylanase-
Palavras-chave: dc.subjectBacillus licheniformis-
Palavras-chave: dc.subjectxylanase purification-
Palavras-chave: dc.subjectalkalophilic bacteria-
Palavras-chave: dc.subjectxylanase characterization-
Título: dc.titlePurification and characterization of two xylanases from alkalophilic and thermophilic Bacillus licheniformis 77-2-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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