Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation

dc.contributor.authorAlves, Thais Barboni [UNESP]
dc.contributor.authorOliveira Ornela, Pedro Henrique de [UNESP]
dc.contributor.authorCavalcanti de Oliveira, Arthur Henrique [UNESP]
dc.contributor.authorJorge, Joao Atilio
dc.contributor.authorSouza Guimaraes, Luis Henrique [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2018-11-26T16:04:41Z
dc.date.available2018-11-26T16:04:41Z
dc.date.issued2018-08-10
dc.description.abstractThe filamentous fungus Aspergillus niveus produced extracellular antifungal chitinase when cultured under submerged fermentation (SbmF) using crab shells as the carbon source. Maximal chitinase production was achieved at 192 h of cultivation using minimal medium containing 1% chitin. The enzyme was purified 1.97-fold with 40% recovery by ammonium sulfate precipitation and Sephadex G-100 gel filtration. The molecular mass was estimated to be 44 kDa by both 12% SDS-PAGE and Sepharose CL-6B gel filtration. Maximal A. niveus chitinase activity was obtained at 65 degrees C and pH 5.0. The enzyme was fully stable at 60 degrees C for up to 120 min and the enzymatic activity was increased by Mn2+. In the presence of reducing and denaturing compounds, the enzyme activity was not drastically affected. The chitinase was able to hydrolyze colloidal chitin, azure chitin, and 4-nitrophenyl N-acetyl-beta-D glucosaminide; for the latter, the K-0.5 and maximal velocity (V-max) were 3.51 mM and 9.68 U/mg of protein, respectively. The A. niveus chitinase presented antifungal activity against Aspergillus niger (MIC = 84 mu g/mL), A. fumigatus (MIC = 21 mu g/mL), A. flavus (MIC = 24 mu g/mL), A. phoenicis (MIC = 24 mu g/mL), and Paecilomyces variotii (MIC = 21 mu g/mL). The fungus A. niveus was able to produce a thermostable and denaturation-resistant chitinase able to inhibit fungal development, signaling its biotechnological potential.en
dc.description.affiliationUniv Estadual Paulista, Inst Quim, Rua Prof Francisco Degni 55, BR-14800900 Araraquara, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Quim, Rua Prof Francisco Degni 55, BR-14800900 Araraquara, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 2011/50880-1
dc.format.extent10
dc.identifierhttp://dx.doi.org/10.1007/s13205-018-1397-6
dc.identifier.citation3 Biotech. Heidelberg: Springer Heidelberg, v. 8, n. 8, 10 p., 2018.
dc.identifier.doi10.1007/s13205-018-1397-6
dc.identifier.issn2190-572X
dc.identifier.urihttp://hdl.handle.net/11449/160489
dc.identifier.wosWOS:000441262700004
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartof3 Biotech
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectAspergillus niveus
dc.subjectAntifungal activity
dc.subjectChitin
dc.subjectChitinase
dc.subjectFungal hydrolases
dc.titleProduction and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentationen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer

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