Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.

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dc.contributor.authorZanphorlin, Leticia Maria [UNESP]
dc.contributor.authorAntonio Facchini, Fernanda Dell
dc.contributor.authorVasconcelos, Filipe [UNESP]
dc.contributor.authorBonugli-Santos, Rafaella Costa
dc.contributor.authorRodrigues, Andre [UNESP]
dc.contributor.authorSette, Lara Duraes
dc.contributor.authorGomes, Eleni [UNESP]
dc.contributor.authorBonilla-Rodriguez, Gustavo Orlando [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.date.accessioned2013-09-30T18:47:32Z
dc.date.accessioned2014-05-20T13:56:26Z
dc.date.available2013-09-30T18:47:32Z
dc.date.available2014-05-20T13:56:26Z
dc.date.issued2010-06-01
dc.description.abstractThermophilic fungi produce thermostable enzymes which have a number of applications, mainly in biotechnological processes. In this work, we describe the characterization of a protease produced in solidstate (SSF) and submerged (SmF) fermentations by a newly isolated thermophilic fungus identified as a putative new species in the genus Myceliophthora. Enzyme-production rate was evaluated for both fermentation processes, and in SSF, using a medium composed of a mixture of wheat bran and casein, the proteolytic output was 4.5-fold larger than that obtained in SmF. Additionally, the peak of proteolytic activity was obtained after 3 days for SSF whereas for SmF it was after 4 days. The crude enzyme obtained by both SSF and SmF displayed similar optimum temperature at 50A degrees C, but the optimum pH shifted from 7 (SmF) to 9(SSF). The alkaline protease produced through solid-state fermentation (SSF), was immobilized on beads of calcium alginate, allowing comparative analyses of free and immobilized proteases to be carried out. It was observed that both optimum temperature and thermal stability of the immobilized enzyme were higher than for the free enzyme. Moreover, the immobilized enzyme showed considerable stability for up to 7 reuses.en
dc.description.affiliationUNESP Univ Estadual Paulista IBILCE, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUSP, BR-14049900 Ribeirao Preto, SP, Brazil
dc.description.affiliationUNICAMP Univ Campinas, CPQBA, Div Microbial Resources, BR-13081970 Campinas, SP, Brazil
dc.description.affiliationUNESP Univ Estadual Paulista, Ctr Study Social Insects, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationUnespUNESP Univ Estadual Paulista IBILCE, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP Univ Estadual Paulista, Ctr Study Social Insects, BR-13506900 Rio Claro, SP, Brazil
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent331-336
dc.identifierhttp://dx.doi.org/10.1007/s12275-010-9269-8
dc.identifier.citationJournal of Microbiology. Seoul: Microbiological Society Korea, v. 48, n. 3, p. 331-336, 2010.
dc.identifier.doi10.1007/s12275-010-9269-8
dc.identifier.issn1225-8873
dc.identifier.orcid0000-0002-4164-9362
dc.identifier.urihttp://hdl.handle.net/11449/20175
dc.identifier.wosWOS:000279087800010
dc.language.isoeng
dc.publisherMicrobiological Society Korea
dc.relation.ispartofJournal of Microbiology
dc.relation.ispartofjcr2.319
dc.relation.ispartofsjr0,911
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectalkaline proteaseen
dc.subjectimmobilized enzymeen
dc.subjectMyceliophthora sp.en
dc.subjectsolid state fermentationen
dc.subjectthermophilic fungusen
dc.titleProduction, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.en
dc.typeResenha
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderMicrobiological Society Korea
unesp.author.lattes8538509657578022[5]
unesp.author.orcid0000-0002-4164-9362[5]

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Rio Claro - CEIS - Centro de Estudos de Insetos Sociais