Analysis of the Specificity and Biochemical Characterization of Metalloproteases Isolated from Eupenicillium javanicum Using Fluorescence Resonance Energy Transfer Peptides

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dc.contributor.author Hamin Neto, Youssef A. A.
dc.contributor.author de oliveira, Lilian C. G.[INIFESP]
dc.contributor.author de oliveira, Juliana R.[INIFESP]
dc.contributor.author Juliano, Maria A.[INIFESP]
dc.contributor.author Juliano, Luiz[INIFESP]
dc.contributor.author Arantes, Eliane C.
dc.contributor.author Cabral, Hamilton
dc.date.accessioned 2020-07-17T14:03:15Z
dc.date.available 2020-07-17T14:03:15Z
dc.date.issued 2017
dc.identifier http://dx.doi.org/10.3389/fmicb.2016.02141
dc.identifier.citation Frontiers In Microbiology. Lausanne, v. 7, p. -, 2017.
dc.identifier.issn 1664-302X
dc.identifier.uri https://repositorio.unifesp.br/handle/11600/55264
dc.description.abstract Enzymes have important features that may facilitate their application in industrial processes and have been used as alternatives to chemical catalysts. In particular, proteases can be isolated from microorganisms, which provide important sources of advantageous enzymes for industrial processes. For example, Eupenicillium javanicum is a filamentous fungus that has been shown to express industrially applicable enzymes and chemical components, such as antifungal compounds. The biotechnological potential of E. javanicum and proteases made us search a novel protease from this microorganism. The macromolecule was isolated, the main biochemical properties was evaluated, and the specificity of the protease subsites was determined. The protease was produced under solid-state bioprocess with wheat bran and isolated by two chromatography steps with yield of 27.5% and 12.4-fold purification. The molecular mass was estimated at 30 kDa. The N-terminal sequence of the first 20 amino acid residues was AVGAGYNASVALALEKALNN. The enzyme presented higher proteolytic activity at pH 6.0 and 60 degrees C. The protease is stable at wide range of pH values and temperatures and in the presence of surfactants. The primed side of the catalytic site showed the highest catalytic efficiency of the enzyme isolated from E. javanicum. The S'(1) subsite is responsible for catalyzing the protease reaction with substrates with tyrosine in P'(1). These findings provide important insights into the biochemical characterization of a highly active protease from E. javanicum and may facilitate the development of industrial processes involving this protease. en
dc.description.sponsorship Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2012/24703-8, 2011/06986-0]
dc.format.extent -
dc.language.iso eng
dc.publisher Frontiers Media Sa
dc.relation.ispartof Frontiers In Microbiology
dc.rights Acesso aberto
dc.subject biochemical characterization en
dc.subject fluorescence resonance energy transfer peptides en
dc.subject microbial enzyme en
dc.subject protease en
dc.subject solid-state fermentation en
dc.title Analysis of the Specificity and Biochemical Characterization of Metalloproteases Isolated from Eupenicillium javanicum Using Fluorescence Resonance Energy Transfer Peptides en
dc.type Artigo
dc.description.affiliation Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Pharmaceut Sci, Ribeirao Preto, Brazil
dc.description.affiliation Univ Fed Sao Paulo, Paulista Med Sch, Dept Biophys, Sao Paulo, Brazil
dc.description.affiliation Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Phys & Chem, Ribeirao Preto, Brazil
dc.description.affiliationUnifesp Univ Fed Sao Paulo, Paulista Med Sch, Dept Biophys, Sao Paulo, Brazil
dc.description.sponsorshipID FAPESP: 2012/24703-8
dc.description.sponsorshipID FAPESP: 2011/06986-0
dc.identifier.file WOS000391497100001.pdf
dc.identifier.doi 10.3389/fmicb.2016.02141
dc.description.source Web of Science
dc.identifier.wos WOS:000391497100001
dc.coverage Lausanne
dc.citation.volume 7



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