Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp.
dc.contributor.author | Zanphorlin, Leticia Maria [UNESP] | |
dc.contributor.author | Antonio Facchini, Fernanda Dell | |
dc.contributor.author | Vasconcelos, Filipe [UNESP] | |
dc.contributor.author | Bonugli-Santos, Rafaella Costa | |
dc.contributor.author | Rodrigues, Andre [UNESP] | |
dc.contributor.author | Sette, Lara Duraes | |
dc.contributor.author | Gomes, Eleni [UNESP] | |
dc.contributor.author | Bonilla-Rodriguez, Gustavo Orlando [UNESP] | |
dc.contributor.institution | Universidade Estadual Paulista (Unesp) | |
dc.contributor.institution | Universidade de São Paulo (USP) | |
dc.contributor.institution | Universidade Estadual de Campinas (UNICAMP) | |
dc.date.accessioned | 2013-09-30T18:47:32Z | |
dc.date.accessioned | 2014-05-20T13:56:26Z | |
dc.date.available | 2013-09-30T18:47:32Z | |
dc.date.available | 2014-05-20T13:56:26Z | |
dc.date.issued | 2010-06-01 | |
dc.description.abstract | Thermophilic 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.affiliation | UNESP Univ Estadual Paulista IBILCE, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliation | USP, BR-14049900 Ribeirao Preto, SP, Brazil | |
dc.description.affiliation | UNICAMP Univ Campinas, CPQBA, Div Microbial Resources, BR-13081970 Campinas, SP, Brazil | |
dc.description.affiliation | UNESP Univ Estadual Paulista, Ctr Study Social Insects, BR-13506900 Rio Claro, SP, Brazil | |
dc.description.affiliationUnesp | UNESP Univ Estadual Paulista IBILCE, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliationUnesp | UNESP Univ Estadual Paulista, Ctr Study Social Insects, BR-13506900 Rio Claro, SP, Brazil | |
dc.description.sponsorship | Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) | |
dc.description.sponsorship | Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) | |
dc.description.sponsorship | Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) | |
dc.format.extent | 331-336 | |
dc.identifier | http://dx.doi.org/10.1007/s12275-010-9269-8 | |
dc.identifier.citation | Journal of Microbiology. Seoul: Microbiological Society Korea, v. 48, n. 3, p. 331-336, 2010. | |
dc.identifier.doi | 10.1007/s12275-010-9269-8 | |
dc.identifier.issn | 1225-8873 | |
dc.identifier.orcid | 0000-0002-4164-9362 | |
dc.identifier.uri | http://hdl.handle.net/11449/20175 | |
dc.identifier.wos | WOS:000279087800010 | |
dc.language.iso | eng | |
dc.publisher | Microbiological Society Korea | |
dc.relation.ispartof | Journal of Microbiology | |
dc.relation.ispartofjcr | 2.319 | |
dc.relation.ispartofsjr | 0,911 | |
dc.rights.accessRights | Acesso restrito | |
dc.source | Web of Science | |
dc.subject | alkaline protease | en |
dc.subject | immobilized enzyme | en |
dc.subject | Myceliophthora sp. | en |
dc.subject | solid state fermentation | en |
dc.subject | thermophilic fungus | en |
dc.title | Production, partial characterization, and immobilization in alginate beads of an alkaline protease from a new thermophilic fungus Myceliophthora sp. | en |
dc.type | Resenha | |
dcterms.license | http://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0 | |
dcterms.rightsHolder | Microbiological Society Korea | |
unesp.author.lattes | 8538509657578022[5] | |
unesp.author.orcid | 0000-0002-4164-9362[5] |
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