Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus

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dc.contributor.authorBiaggio, Rafael Tage
dc.contributor.authorSilva, Ronivaldo Rodrigues da [UNESP]
dc.contributor.authorRosa, Nathalia Gonsales da
dc.contributor.authorRibeiro Leite, Rodrigo Simoes
dc.contributor.authorArantes, Eliane Candiani
dc.contributor.authorFreitas Cabral, Tatiana Pereira de
dc.contributor.authorJuliano, Maria A.
dc.contributor.authorJuliano, Luiz
dc.contributor.authorCabral, Hamilton
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionFed Univ Grande Dourados
dc.contributor.institutionUniv Ctr Educ Fdn Barretos
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2018-11-26T15:29:22Z
dc.date.available2018-11-26T15:29:22Z
dc.date.issued2016-01-01
dc.description.abstractPeptidases are important because they play a central role in pharmaceutical, food, environmental, and other industrial processes. A serine peptidase from Aspergillus terreus was isolated after two chromatography steps that showed a yield of 15.5%. Its molecular mass was determined to be 43 kD, by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). This peptidase was active between pH 5.0 to 8.0 and had maximum activity at pH 7.0, at 45 degrees C. When exposited with 1 M of urea, the enzyme maintained 100% activity and used azocasein as substrate. The N-terminal (first 15 residues) showed 33% identity with the serine peptidase of Aspergillus clavatus ES1. The kinetics assays showed that subsite S-2 did not bind polar basic amino acids (His and Arg) nonpolar acidic amino acids (Asp and Glu). The subsite S-1 showed higher catalytic efficiency than the S-2 and S-3 subsites.en
dc.description.affiliationUniv Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Pharmaceut Sci, S-N Cafe, BR-14040903 Ribeirao Preto, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Biosci Letters & Exact Sci, Sao Jose Do Rio Preto, Brazil
dc.description.affiliationFed Univ Grande Dourados, Fac Biol & Environm Sci, Dourados, Brazil
dc.description.affiliationUniv Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Chem & Phys, BR-14040903 Ribeirao Preto, Brazil
dc.description.affiliationUniv Ctr Educ Fdn Barretos, Fac Pharm, Barretos, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Paulista Sch Med, Dept Biophys, Sao Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biosci Letters & Exact Sci, Sao Jose Do Rio Preto, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPESP: 2011/06986-0
dc.description.sponsorshipIdFAPESP: 2012/24703-8
dc.description.sponsorshipIdCNPq: 308078/2012-8
dc.format.extent298-304
dc.identifierhttp://dx.doi.org/10.1080/10826068.2015.1031387
dc.identifier.citationPreparative Biochemistry & Biotechnology. Philadelphia: Taylor & Francis Inc, v. 46, n. 3, p. 298-304, 2016.
dc.identifier.doi10.1080/10826068.2015.1031387
dc.identifier.fileWOS000374887000012.pdf
dc.identifier.issn1082-6068
dc.identifier.urihttp://hdl.handle.net/11449/158832
dc.identifier.wosWOS:000374887000012
dc.language.isoeng
dc.publisherTaylor & Francis Inc
dc.relation.ispartofPreparative Biochemistry & Biotechnology
dc.relation.ispartofsjr0,362
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectAspergillus
dc.subjectenzyme kinetics
dc.subjectfilamentous fungi
dc.subjectN-terminal sequence
dc.subjectprotease
dc.subjectprotein
dc.titlePurification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreusen
dc.typeArtigo
dcterms.licensehttp://journalauthors.tandf.co.uk/permissions/reusingOwnWork.asp
dcterms.rightsHolderTaylor & Francis Inc
unesp.author.orcid0000-0002-5589-2822[8]
unesp.author.orcid0000-0002-7365-1694[9]

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