Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide

Lipases from Candida antarctica and Mucor miehei were encapsulated in lecithin water-in-oil (w/o) microemulsion-based organogels (MBG). These gels were formulated with either hydroxypropylmethyl cellulose (HPMC) or gelatin. The esterification of lauric acid and 1-propanol catalyzed by these MBGs was...

Full description

Bibliographic Details
Main Authors: Blattner, Christian, Zoumpanioti, Maria, Kröner, Jürgen, Schmeer, Georg, Xenakis, Aristotelis, Kunz, Werner
Format: Text
Language:unknown
Published: Universität Regensburg 2006
Subjects:
Online Access:https://dx.doi.org/10.5283/epub.7
https://epub.uni-regensburg.de/id/eprint/7
id ftdatacite:10.5283/epub.7
record_format openpolar
spelling ftdatacite:10.5283/epub.7 2023-05-15T13:39:22+02:00 Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide Blattner, Christian Zoumpanioti, Maria Kröner, Jürgen Schmeer, Georg Xenakis, Aristotelis Kunz, Werner 2006 https://dx.doi.org/10.5283/epub.7 https://epub.uni-regensburg.de/id/eprint/7 unknown Universität Regensburg http://dx.doi.org/10.1016/j.supflu.2005.06.007 http://dx.doi.org/10.1016/j.supflu.2005.06.007 https://dx.doi.org/10.1016/j.supflu.2005.06.007 Microemulsion; Organogels; Lipases; Enzymatic reaction; Supercritical CO2 530 Physik 540 Chemie Text Article article-journal ScholarlyArticle 2006 ftdatacite https://doi.org/10.5283/epub.7 https://doi.org/10.1016/j.supflu.2005.06.007 2021-11-05T12:55:41Z Lipases from Candida antarctica and Mucor miehei were encapsulated in lecithin water-in-oil (w/o) microemulsion-based organogels (MBG). These gels were formulated with either hydroxypropylmethyl cellulose (HPMC) or gelatin. The esterification of lauric acid and 1-propanol catalyzed by these MBGs was examined in supercritical carbon dioxide (scCO2; 35◦C, 110 bar) as solvent for the substrates. The results were compared to those obtained with the reference substrate solvent isooctane. It turned out that the initial rates of this model reaction in scCO2 were higher than those observed in the reference system. Various parameters affecting the biocatalysis such as pressure, alcohol and acid chain length, and gel composition were investigated. Kinetic studies showed that the ester synthesis catalyzed by the immobilized C. antarctica lipase occurs via a Ping Pong Bi Bi mechanism in which only inhibition by excess of alcohol was identified. Values of all kinetic parameters were determined. In addition, experiments on the reusability of these gels in scCO2 were carried out and the state of water within the organogel was examined with the help of differential scanning calorimetry. The present study shows that biocatalysis using MBGs in scCO2 is a promising alternative to other bioconversion processes. Text Antarc* Antarctica DataCite Metadata Store (German National Library of Science and Technology)
institution Open Polar
collection DataCite Metadata Store (German National Library of Science and Technology)
op_collection_id ftdatacite
language unknown
topic Microemulsion; Organogels; Lipases; Enzymatic reaction; Supercritical CO2
530 Physik
540 Chemie
spellingShingle Microemulsion; Organogels; Lipases; Enzymatic reaction; Supercritical CO2
530 Physik
540 Chemie
Blattner, Christian
Zoumpanioti, Maria
Kröner, Jürgen
Schmeer, Georg
Xenakis, Aristotelis
Kunz, Werner
Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
topic_facet Microemulsion; Organogels; Lipases; Enzymatic reaction; Supercritical CO2
530 Physik
540 Chemie
description Lipases from Candida antarctica and Mucor miehei were encapsulated in lecithin water-in-oil (w/o) microemulsion-based organogels (MBG). These gels were formulated with either hydroxypropylmethyl cellulose (HPMC) or gelatin. The esterification of lauric acid and 1-propanol catalyzed by these MBGs was examined in supercritical carbon dioxide (scCO2; 35◦C, 110 bar) as solvent for the substrates. The results were compared to those obtained with the reference substrate solvent isooctane. It turned out that the initial rates of this model reaction in scCO2 were higher than those observed in the reference system. Various parameters affecting the biocatalysis such as pressure, alcohol and acid chain length, and gel composition were investigated. Kinetic studies showed that the ester synthesis catalyzed by the immobilized C. antarctica lipase occurs via a Ping Pong Bi Bi mechanism in which only inhibition by excess of alcohol was identified. Values of all kinetic parameters were determined. In addition, experiments on the reusability of these gels in scCO2 were carried out and the state of water within the organogel was examined with the help of differential scanning calorimetry. The present study shows that biocatalysis using MBGs in scCO2 is a promising alternative to other bioconversion processes.
format Text
author Blattner, Christian
Zoumpanioti, Maria
Kröner, Jürgen
Schmeer, Georg
Xenakis, Aristotelis
Kunz, Werner
author_facet Blattner, Christian
Zoumpanioti, Maria
Kröner, Jürgen
Schmeer, Georg
Xenakis, Aristotelis
Kunz, Werner
author_sort Blattner, Christian
title Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
title_short Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
title_full Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
title_fullStr Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
title_full_unstemmed Biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
title_sort biocatalysis using lipase encapsulated in microemulsion-based organogels in supercritical carbon dioxide
publisher Universität Regensburg
publishDate 2006
url https://dx.doi.org/10.5283/epub.7
https://epub.uni-regensburg.de/id/eprint/7
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation http://dx.doi.org/10.1016/j.supflu.2005.06.007
http://dx.doi.org/10.1016/j.supflu.2005.06.007
https://dx.doi.org/10.1016/j.supflu.2005.06.007
op_doi https://doi.org/10.5283/epub.7
https://doi.org/10.1016/j.supflu.2005.06.007
_version_ 1766117813730148352