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dc.creatorRomero, Cintia Mariana-
dc.creatorPera, Licia Maria-
dc.creatorLoto, Flavia del Valle-
dc.creatorCostas, Luciana-
dc.creatorBaigori, Mario Domingo-
dc.date2015-08-24T14:51:12Z-
dc.date2015-08-24T14:51:12Z-
dc.date2013-02-02-
dc.date2016-03-30 10:35:44.97925-03-
dc.date.accessioned2019-04-29T15:40:37Z-
dc.date.available2019-04-29T15:40:37Z-
dc.date.issued2015-08-24T14:51:12Z-
dc.date.issued2015-08-24T14:51:12Z-
dc.date.issued2013-02-02-
dc.date.issued2016-03-30 10:35:44.97925-03-
dc.identifierRomero, Cintia Mariana; Pera, Licia Maria; Loto, Flavia del Valle; Costas, Luciana; Baigori, Mario Domingo; Pretreatment of an induced mycelium-bound lipase from Arpergillus niger MYA 135 improves its hydrolytic and synthetic activity; Springer; Catalysis Letters; 143; 5; 02-2-2013; 469-475-
dc.identifier1011-372X-
dc.identifierhttp://hdl.handle.net/11336/1786-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/299245-
dc.descriptionWhole-cell enzymes have been used as biocatalysts in a variety of reactions, such as free fatty acid production and the synthesis of fatty acid esters. In the present study, enzyme pretreatments with PEG, MES, Tween 80, Saponine, MgCl 2.H2O, CaCl2 and different pH values were evaluated by using the Plackett-Burman statistical design to improve both the hydrolytic and synthetic activity of an induced mycelium-bound lipase from Aspergillus niger MYA 135. Interestingly, the preincubation at pH 4 had a significant effect on both the hydrolytic and transesterification activity, demonstrating the influence of the correct ionisation state on these activities. Meanwhile, the enzyme pretreatment with MgCl2 for in situ water activity control positively affected the esterification catalyst. Thus, compared with the control without pretreatment, the hydrolytic and the transesterification activities increased to 60.1 and 60.8 %, respectively, and with respect to the esterification reaction, the conversion was improved 2.33 times. Based on these results, by applying a simple pretreatment to the biocatalyst, the catalyst's activity toward hydrolysis and synthesis was enhanced.-
dc.descriptionFil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina; Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina;-
dc.descriptionFil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina;-
dc.descriptionFil: Loto, Flavia del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina;-
dc.descriptionFil: Costas, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina;-
dc.descriptionFil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina; Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina;-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherSpringer-
dc.relation© Springer Science+Business Media New York 2013-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/DOI:10.1007/s10562-013-0966-x-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs10562-013-0966-x-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectPLACKETT-BURMAN-
dc.subjectMYCELIUM-BOUND LIPASE-
dc.subjectHYDROLYSIS-
dc.subjectSYNTHESIS-
dc.subjectASPERGILLUS NIGER-
dc.subjectBioprocesamiento Tecnológico, Biocatálisis, Fermentación-
dc.subjectBiotecnología Industrial-
dc.subjectINGENIERÍAS Y TECNOLOGÍAS-
dc.titlePretreatment of an induced mycelium-bound lipase from Arpergillus niger MYA 135 improves its hydrolytic and synthetic activity-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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