Biochemical and Functional Characterization of a Metalloprotease from the Thermophilic Fungus Thermoascus aurantiacus

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorMerheb-Dini, Carolina-
Autor(es): dc.creatorCabral, Hamilton-
Autor(es): dc.creatorLeite, Rodrigo S. R.-
Autor(es): dc.creatorZanphorlin, Leticia M.-
Autor(es): dc.creatorOkamoto, Debora N.-
Autor(es): dc.creatorBonilla-Rodriguez, Gustavo Orlando-
Autor(es): dc.creatorJuliano, Luiz-
Autor(es): dc.creatorArantes, Eliane C.-
Autor(es): dc.creatorGomes, Eleni-
Autor(es): dc.creatorda Silva, Roberto-
Data de aceite: dc.date.accessioned2021-03-10T17:19:54Z-
Data de disponibilização: dc.date.available2021-03-10T17:19:54Z-
Data de envio: dc.date.issued2014-05-20-
Data de envio: dc.date.issued2014-05-20-
Data de envio: dc.date.issued2009-10-14-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1021/jf9017977-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/21609-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/21609-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionCNPq: 151868/2006-9-
Descrição: dc.descriptionProtease production was carried out in solid state fermentation. The enzyme was purified through precipitation with ethanol at 72% followed by chromatographies in columns of Sephadex G75 and Sephacryl S100. It was purified 80-fold and exhibited recovery of total activity of 0.4%. SDS-PAGE analysis indicated an estimated molecular mass of 24.5 kDa and the N-terminal sequence of the first 22 residues was APYSGYQCSMQLCLTCALMNCA. Purified protease was only inhibited by EDTA (96.7%) and stimulated by Fe(2+) revealing to be a metalloprotease activated by iron. Optimum pH was 5.5, optimum temperature was 75 degrees C, and it was thermostable at 65 degrees C for 1 h maintaining more than 70% of original activity. Through enzyme kinetic studies, protease better hydrolyzed casein than azocasein. The screening of fluorescence resonance energy transfer (FRET) peptide series derived from Abz-KLXSSKQ-EDDnp revealed that the enzyme exhibited preference for Arg in P(1) (k(cat)/K(m) = 30.1 mM(-1) s(-1)).-
Formato: dc.format9210-9217-
Idioma: dc.languageen-
Publicador: dc.publisherAmer Chemical Soc-
Relação: dc.relationJournal of Agricultural and Food Chemistry-
Relação: dc.relation3.412-
Relação: dc.relation1,269-
Direitos: dc.rightsclosedAccess-
Palavras-chave: dc.subjectThermoascus aurantiacus-
Palavras-chave: dc.subjectSolid state fermentation (SSF)-
Palavras-chave: dc.subjectmetalloprotease-
Palavras-chave: dc.subjectThermostability-
Palavras-chave: dc.subjectfluorescent peptides-
Palavras-chave: dc.subjectN-terminal sequence-
Título: dc.titleBiochemical and Functional Characterization of a Metalloprotease from the Thermophilic Fungus Thermoascus aurantiacus-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

Não existem arquivos associados a este item.