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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/76115
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dc.contributor.authorAndrade, Milena M.-
dc.contributor.authorBarbosa, Aneli M.-
dc.contributor.authorBofinger, Matheus R.-
dc.contributor.authorDekker, Robert F. H.-
dc.contributor.authorMessias, Josana M.-
dc.contributor.authorGuedes, Carmen L. B.-
dc.contributor.authorZaminelli, Tiago-
dc.contributor.authorDe Oliveira, Bruno H.-
dc.contributor.authorDe Lima, Valéria M. G.-
dc.contributor.authorDall'Antonia, Luiz H.-
dc.date.accessioned2014-05-27T11:30:05Z-
dc.date.accessioned2016-10-25T18:51:55Z-
dc.date.available2014-05-27T11:30:05Z-
dc.date.available2016-10-25T18:51:55Z-
dc.date.issued2013-08-01-
dc.identifierhttp://dx.doi.org/10.1007/s12010-013-0309-9-
dc.identifier.citationApplied Biochemistry and Biotechnology, v. 170, n. 7, p. 1792-1806, 2013.-
dc.identifier.issn0273-2289-
dc.identifier.issn1559-0291-
dc.identifier.urihttp://hdl.handle.net/11449/76115-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/76115-
dc.description.abstractThe effects of soybean and castorbean meals were evaluated separately, and in combinations at different ratios, as substrates for lipase production by Botryosphaeria ribis EC-01 in submerged fermentation using only distilled water. The addition of glycerol analytical grade (AG) and glycerol crude (CG) to soybean and castorbean meals separately and in combination, were also examined for lipase production. Glycerol-AG increased enzyme production, whereas glycerol-CG decreased it. A 24 factorial design was developed to determine the best concentrations of soybean meal, castorbean meal, glycerol-AG, and KH2PO4 to optimize lipase production by B. ribis EC-01. Soybean meal and glycerol-AG had a significant effect on lipase production, whereas castorbean meal did not. A second treatment (22 factorial design central composite) was developed, and optimal lipase production (4,820 U/g of dry solids content (ds)) was obtained when B. ribis EC-01 was grown on 0.5 % (w/v) soybean meal and 5.2 % (v/v) glycerol in distilled water, which was in agreement with the predicted value (4,892 U/g ds) calculated by the model. The unitary cost of lipase production determined under the optimized conditions developed ranged from US$0.42 to 0.44 based on nutrient costs. The fungal lipase was immobilized onto Celite and showed high thermal stability and was used for transesterification of soybean oil in methanol (1:3) resulting in 36 % of fatty acyl alkyl ester content. The apparent K m and V max were determined and were 1.86 mM and 14.29 μmol min -1 mg-1, respectively. © 2013 Springer Science+Business Media New York.en
dc.format.extent1792-1806-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectAgro-industrial residues-
dc.subjectCelite-
dc.subjectGlycerol-
dc.subjectImmobilization-
dc.subjectLipase production-
dc.subjectResponse surface method-
dc.subjectSubmerged fermentation-
dc.subjectAgro-industrial residue-
dc.subjectFermentation-
dc.subjectOptimization-
dc.subjectRadioactive waste vitrification-
dc.subjectSubstrates-
dc.subjectalkyl group-
dc.subjectbiodiesel-
dc.subjectester-
dc.subjectglycerol-
dc.subjectinfusorial earth-
dc.subjectmethanol-
dc.subjectsoybean oil-
dc.subjecttriacylglycerol lipase-
dc.subjectwater-
dc.subjectbean-
dc.subjectbiofuel production-
dc.subjectBotryosphaeria ribis-
dc.subjectcastorbean-
dc.subjectenzyme immobilization-
dc.subjectenzyme kinetics-
dc.subjectenzyme synthesis-
dc.subjectfactorial design-
dc.subjectfungus-
dc.subjectmeal-
dc.subjectnonhuman-
dc.subjectnucleotide sequence-
dc.subjectnutrient-
dc.subjectpredictive value-
dc.subjectresponse surface method-
dc.subjectsoybean-
dc.subjectsubmerged fermentation-
dc.subjectGlycine max-
dc.subjectRicinus communis-
dc.titleLipase production by Botryosphaeria ribis EC-01 on soybean and castorbean meals: Optimization, immobilization, and application for biodiesel productionen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual de Londrina (UEL)-
dc.contributor.institutionLakehead University-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.description.affiliationDepartamento de Química CCE Universidade Estadual de Londrina, 86051-990 Londrina, Parana-
dc.description.affiliationDepartamento de Bioquímica e Biotecnologia CCE-Universidade Estadual de Londrina, 86051-990 Londrina, Parana-
dc.description.affiliationBiorefining Research Institute Lakehead University, Thunder Bay, ON P7B 5E1-
dc.description.affiliationDepartamento de Ciências Biológicas Universidade Estadual Paulista (UNESP), 19806-900 Assis, São Paulo-
dc.description.affiliationDepartamento de Bioquímica e Imunologia FMRP-Universidade de São Paulo, 14049-900 Ribeirão Preto, São Paulo-
dc.description.affiliationUnespDepartamento de Ciências Biológicas Universidade Estadual Paulista (UNESP), 19806-900 Assis, São Paulo-
dc.identifier.doi10.1007/s12010-013-0309-9-
dc.identifier.wosWOS:000322542900020-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofApplied Biochemistry and Biotechnology-
dc.identifier.scopus2-s2.0-84881233696-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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