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dc.contributor.author
Romero, Cintia Mariana
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Pera, Licia Maria
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Loto, Flavia del Valle
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Costas, Luciana
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Baigori, Mario Domingo
dc.date.available
2015-08-24T14:51:12Z
dc.date.issued
2013-02-02
dc.identifier.citation
Romero, 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.identifier.issn
1011-372X
dc.identifier.uri
http://hdl.handle.net/11336/1786
dc.description.abstract
Whole-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.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.relation
© Springer Science+Business Media New York 2013
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Plackett-Burman
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Mycelium-Bound Lipase
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Hydrolysis
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Synthesis
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Aspergillus Niger
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Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
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Biotecnología Industrial
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Pretreatment of an induced mycelium-bound lipase from Arpergillus niger MYA 135 improves its hydrolytic and synthetic activity
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-30 10:35:44.97925-03
dc.journal.volume
143
dc.journal.number
5
dc.journal.pagination
469-475
dc.journal.pais
Alemania
dc.journal.ciudad
Berlin
dc.description.fil
Fil: 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.description.fil
Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina;
dc.description.fil
Fil: 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.description.fil
Fil: Costas, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET- Tucumán. Planta Piloto de Procesos Industriales Microbiológicos (i); Argentina;
dc.description.fil
Fil: 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.journal.title
Catalysis Letters
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/DOI:10.1007/s10562-013-0966-x
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info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs10562-013-0966-x