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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/116669
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dc.contributor.authorFerrarezi, Ana Lucia-
dc.contributor.authorKobe Ohe, Thiago Hideyuki-
dc.contributor.authorBorges, Janaina Pires-
dc.contributor.authorBrito, Rafaela Rodrigues-
dc.contributor.authorSiqueira, Marcos Rechi-
dc.contributor.authorVendramini, Pedro Henrique-
dc.contributor.authorQuilles, Jose Carlos-
dc.contributor.authorCarreira Nunes, Christiane da Costa-
dc.contributor.authorBonilla-Rodriguez, Gustavo Orlando-
dc.contributor.authorBoscolo, Mauricio-
dc.contributor.authorDa-Silva, Roberto-
dc.contributor.authorGomes, Eleni-
dc.date.accessioned2015-03-18T15:53:42Z-
dc.date.accessioned2016-10-25T20:25:20Z-
dc.date.available2015-03-18T15:53:42Z-
dc.date.available2016-10-25T20:25:20Z-
dc.date.issued2014-09-01-
dc.identifierhttp://dx.doi.org/10.1016/j.molcatb.2014.05.012-
dc.identifier.citationJournal Of Molecular Catalysis B-enzymatic. Amsterdam: Elsevier Science Bv, v. 107, p. 106-113, 2014.-
dc.identifier.issn1381-1177-
dc.identifier.urihttp://hdl.handle.net/11449/116669-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/116669-
dc.description.abstractAmong 54 thermophilic fungi tested for lipase production, the highest yield was obtained for Thermomucor indicae seudaticae in submerged (SmF) and solid state fermentation (SSF), being that species selected for studies of fermentative parameters. Some modifications of the culture media afforded an improvement of 15 fold in the lipase activity in SSF and 8 fold in SmF. Furthermore, the lipases produced through both SSF and SmF exhibited maximum lipolytic activity at 40 degrees C but these lipases were different since the enzyme from SmF presented maximum activity at neutral pH (6.0-7.0) whereas the lipase from SSF displayed maximum activity at acidic pH (3.0-4.0). The fungus was grown on loofah sponges, and the immobilized hyphae showed 108 U g - lipolytic activity, a profile including both alkaline and acidic activities. The esterification and transesterification yields were 28% and 13.2% using oleic acid and soybean oil, respectively. Those are essential reactions for biodiesel production. Thus, the lipase production of both the immobilized whole cells as well as the cultivated fungus T. indicae seudaticae N31 may be considered promising in synthesis reactions. (C) 2014 Elsevier B.V. All rights reserved.en
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.format.extent106-113-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectThermomucor indicae seudaticaeen
dc.subjectLipaseen
dc.subjectSubmerged fermentationen
dc.subjectSolid state fermentationen
dc.subjectWhole cellen
dc.subjectTransesterification reactionen
dc.titleProduction and characterization of lipases and immobilization of whole cell of the thermophilic Thermomucor indicae seudaticae N31 for transesterification reactionen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUNESP Univ Estadual Paulista, IBILCE, Lab Bioquim Microbiol Aplicada, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP Univ Estadual Paulista, IBILCE, Lab Sucroquim, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP Univ Estadual Paulista, IBILCE, Lab Sucroquim & Quim Analit, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP Univ Estadual Paulista, IBILCE, Lab Bioquim Microbiol Aplicada, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP Univ Estadual Paulista, IBILCE, Lab Sucroquim, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP Univ Estadual Paulista, IBILCE, Lab Sucroquim & Quim Analit, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.identifier.doi10.1016/j.molcatb.2014.05.012-
dc.identifier.wosWOS:000340698300015-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal Of Molecular Catalysis B-enzymatic-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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