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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  
dc.subject
Naringinase  
dc.subject
Liquid-Liquid Biocatalisis  
dc.subject.classification
Ingeniería Química  
dc.subject.classification
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