Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens

Autores
Magario, Ivana; Vielhauer, Oliver; Neumann, Anke; Hausmann, Rudolf; Syldatk, Christoph
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
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
Fil: Vielhauer, Oliver. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Fil: Neumann, Anke. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Fil: Hausmann, Rudolf. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Fil: Syldatk, Christoph. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Materia
Rhamnolipds
Micellar Substrates
Naringinase
Liquid-Liquid Biocatalisis
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/20740
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/20740
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbensMagario, IvanaVielhauer, OliverNeumann, AnkeHausmann, RudolfSyldatk, ChristophRhamnolipdsMicellar SubstratesNaringinaseLiquid-Liquid Biocatalisishttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2The 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.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.; ArgentinaFil: Vielhauer, Oliver. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; AlemaniaFil: Neumann, Anke. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; AlemaniaFil: Hausmann, Rudolf. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; AlemaniaFil: Syldatk, Christoph. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; AlemaniaJohn Wiley & Sons Inc2009-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/20740Magario, 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; 9-190006-3592CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www3.interscience.wiley.com/journal/121356482/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1002/bit.22057info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:55:04Zoai:ri.conicet.gov.ar:11336/20740instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:55:04.315CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
title Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
spellingShingle Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
Magario, Ivana
Rhamnolipds
Micellar Substrates
Naringinase
Liquid-Liquid Biocatalisis
title_short Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
title_full Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
title_fullStr Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
title_full_unstemmed Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
title_sort Kinetic Analysis and Modeling of the Liquid–Liquid Conversion of emulsified di-rhamnolipids by Naringinase from Penicillium decumbens
dc.creator.none.fl_str_mv Magario, Ivana
Vielhauer, Oliver
Neumann, Anke
Hausmann, Rudolf
Syldatk, Christoph
author Magario, Ivana
author_facet Magario, Ivana
Vielhauer, Oliver
Neumann, Anke
Hausmann, Rudolf
Syldatk, Christoph
author_role author
author2 Vielhauer, Oliver
Neumann, Anke
Hausmann, Rudolf
Syldatk, Christoph
author2_role author
author
author
author
dc.subject.none.fl_str_mv Rhamnolipds
Micellar Substrates
Naringinase
Liquid-Liquid Biocatalisis
topic Rhamnolipds
Micellar Substrates
Naringinase
Liquid-Liquid Biocatalisis
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv 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.
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
Fil: Vielhauer, Oliver. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Fil: Neumann, Anke. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Fil: Hausmann, Rudolf. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
Fil: Syldatk, Christoph. University of Karlsruhe. Institute of Engineering in Life Sciences. Section of Technical Biology; Alemania
description 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.
publishDate 2009
dc.date.none.fl_str_mv 2009-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/20740
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
0006-3592
CONICET Digital
CONICET
url http://hdl.handle.net/11336/20740
identifier_str_mv 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
0006-3592
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www3.interscience.wiley.com/journal/121356482/abstract
info:eu-repo/semantics/altIdentifier/doi/10.1002/bit.22057
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Inc
publisher.none.fl_str_mv John Wiley & Sons Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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