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dc.contributor.author
Magario, Ivana

dc.contributor.author
Vielhauer, Oliver
dc.contributor.author
Neumann, Anke
dc.contributor.author
Hausmann, Rudolf
dc.contributor.author
Syldatk, Christoph
dc.date.available
2017-07-17T20:20:24Z
dc.date.issued
2009-01
dc.identifier.citation
Magario, Ivana; Vielhauer, Oliver; Neumann, Anke; Hausmann, Rudolf; Syldatk, Christoph; Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens; John Wiley & Sons Inc; Bioengineering And Biotechnology; 102; 1; 1-2009; 9-19
dc.identifier.issn
0006-3592
dc.identifier.uri
http://hdl.handle.net/11336/20740
dc.description.abstract
The enzymatic conversion of an aggregates building substrate was kinetically analyzed and a model was applied for the prediction of reaction-time courses. An L-rhamnose molecule from a di-rhamnolipid is cleaved by Naringinase from Penicillium decumbens leading to a mono-rhamnolipid. Optimal reaction rates were found when both, substrate and product build large co-aggregates in a slightly acidic aqueous phase. On the other hand, reaction rates were independent of initial di-rhamnolipid concentration and this was interpreted by assuming that the reaction occurs in the aqueous phase according to Michaelis–Menten kinetics in combination with competitive L-rhamnose inhibition. Rhamnolipids were therefore assumed to be highly concentrated in aggregates, a second liquid phase, whereas diffusive rhamnolipid transport from and to the aqueous phase occurs due to the enzymatic reaction. Furthermore, ideal surfactant mixing between di- and mono-rhamnolipid was assumed for interpretation of the negative effect of the last on the reaction rate. A model was created that describes the system accordingly. The comparison of the experimental data, were in excellent agreement with the predicted values. The findings of this study may beneficially be adapted for any bioconversions involving aggregate-forming substrate and/or product being catalyzed by hydrophilic enzymes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
John Wiley & Sons Inc

dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Rhamnolipds
dc.subject
Micellar Substrates
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Naringinase
dc.subject
Liquid-Liquid Biocatalisis
dc.subject.classification
Ingeniería Química

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Ingeniería Química

dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS

dc.title
Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-07-13T18:26:33Z
dc.journal.volume
102
dc.journal.number
1
dc.journal.pagination
9-19
dc.journal.pais
Estados Unidos

dc.journal.ciudad
Hoboken
dc.description.fil
Fil: Magario, Ivana. Universidad Nacional de Córdoba. Instituto de Investigación y Desarrollo En Ingeniería de Procesos y Química Aplicada. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación y Desarrollo En Ingeniería de Procesos y Química Aplicada.; Argentina
dc.description.fil
Fil: Vielhauer, Oliver. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
dc.description.fil
Fil: Neumann, Anke. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
dc.description.fil
Fil: Hausmann, Rudolf. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
dc.description.fil
Fil: Syldatk, Christoph. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
dc.journal.title
Bioengineering And Biotechnology

dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www3.interscience.wiley.com/journal/121356482/abstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/bit.22057
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