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

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dc.citation.volume7
dc.contributor.authorHamin Neto, Youssef A. A.
dc.contributor.authorde oliveira, Lilian C. G.[INIFESP]
dc.contributor.authorde oliveira, Juliana R.[INIFESP]
dc.contributor.authorJuliano, Maria A.[INIFESP]
dc.contributor.authorJuliano, Luiz[INIFESP]
dc.contributor.authorArantes, Eliane C.
dc.contributor.authorCabral, Hamilton
dc.coverageLausanne
dc.date.accessioned2020-07-17T14:03:15Z
dc.date.available2020-07-17T14:03:15Z
dc.date.issued2017
dc.description.abstractEnzymes 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.affiliationUniv Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Pharmaceut Sci, Ribeirao Preto, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Paulista Med Sch, Dept Biophys, Sao Paulo, Brazil
dc.description.affiliationUniv Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Phys & Chem, Ribeirao Preto, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Paulista Med Sch, Dept Biophys, Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2012/24703-8, 2011/06986-0]
dc.description.sponsorshipIDFAPESP: 2012/24703-8
dc.description.sponsorshipIDFAPESP: 2011/06986-0
dc.format.extent-
dc.identifierhttp://dx.doi.org/10.3389/fmicb.2016.02141
dc.identifier.citationFrontiers In Microbiology. Lausanne, v. 7, p. -, 2017.
dc.identifier.doi10.3389/fmicb.2016.02141
dc.identifier.fileWOS000391497100001.pdf
dc.identifier.issn1664-302X
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/55264
dc.identifier.wosWOS:000391497100001
dc.language.isoeng
dc.publisherFrontiers Media Sa
dc.relation.ispartofFrontiers In Microbiology
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectbiochemical characterizationen
dc.subjectfluorescence resonance energy transfer peptidesen
dc.subjectmicrobial enzymeen
dc.subjectproteaseen
dc.subjectsolid-state fermentationen
dc.titleAnalysis of the Specificity and Biochemical Characterization of Metalloproteases Isolated from Eupenicillium javanicum Using Fluorescence Resonance Energy Transfer Peptidesen
dc.typeinfo:eu-repo/semantics/article
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