Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B

The preparation of cross‐linked enzyme aggregates (CLEAs) with albumin as an additive is demonstrated successfully with lipase Thermomyces lanuginosus (TL) and lipase B of Candida antarctica (CalB). Investigations regarding the albumin admixture and the temperature optimum are employed. Compared to...

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Published in:European Journal of Lipid Science and Technology
Main Authors: Schroeck, Andrea Maria, Schober, Sigurd, Mittelbach, Martin
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2013
Subjects:
Online Access:http://dx.doi.org/10.1002/ejlt.201300015
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spelling crwiley:10.1002/ejlt.201300015 2024-06-23T07:47:01+00:00 Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B Schroeck, Andrea Maria Schober, Sigurd Mittelbach, Martin 2013 http://dx.doi.org/10.1002/ejlt.201300015 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fejlt.201300015 https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejlt.201300015 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ejlt.201300015 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Lipid Science and Technology volume 115, issue 10, page 1164-1172 ISSN 1438-7697 1438-9312 journal-article 2013 crwiley https://doi.org/10.1002/ejlt.201300015 2024-06-13T04:22:34Z The preparation of cross‐linked enzyme aggregates (CLEAs) with albumin as an additive is demonstrated successfully with lipase Thermomyces lanuginosus (TL) and lipase B of Candida antarctica (CalB). Investigations regarding the albumin admixture and the temperature optimum are employed. Compared to non‐cross‐linked lipase, CalB delivers the best results at a mass ratio of 1:16 lipase/albumin, which leads to a 24‐fold increase of activity; TL at a mass ratio of 1:12, which leads to a eightfold increased activity. A transesterification yield of 61% m/m ethyl ester can be reached with 2.5% m/m CLEAs of lipase TL applied on rapeseed oil within 1.5 h reaction time. A catalyst mass of 10% m/m yields 94% m/m ethyl ester in the same time. Within six cycles of reuse, the catalyst remains stable. CLEAs of CalB and Novozym 435 (a commercial immobilized lipase B of C. antarctica ) show comparable rates in ethanolysis and glycerolysis reaction. Practical applications: CLEAs have become of increasing interest in terms of synthesis of organic compounds via bio‐catalytic (green) approaches. The findings presented here are targeting at transesterification of fats and oils into corresponding alkyl esters applicable, e.g., as alternative fuel substitutes. High conversion rates coupled with hyperactivation effects as well as highly appealing reusability behavior indicate the practical benefits even for technical applications. Conversion of lipids into derivatives by CLEAs as demonstrated here, might extend utilization and conversion possibilities of biomass. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library European Journal of Lipid Science and Technology n/a n/a
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language English
description The preparation of cross‐linked enzyme aggregates (CLEAs) with albumin as an additive is demonstrated successfully with lipase Thermomyces lanuginosus (TL) and lipase B of Candida antarctica (CalB). Investigations regarding the albumin admixture and the temperature optimum are employed. Compared to non‐cross‐linked lipase, CalB delivers the best results at a mass ratio of 1:16 lipase/albumin, which leads to a 24‐fold increase of activity; TL at a mass ratio of 1:12, which leads to a eightfold increased activity. A transesterification yield of 61% m/m ethyl ester can be reached with 2.5% m/m CLEAs of lipase TL applied on rapeseed oil within 1.5 h reaction time. A catalyst mass of 10% m/m yields 94% m/m ethyl ester in the same time. Within six cycles of reuse, the catalyst remains stable. CLEAs of CalB and Novozym 435 (a commercial immobilized lipase B of C. antarctica ) show comparable rates in ethanolysis and glycerolysis reaction. Practical applications: CLEAs have become of increasing interest in terms of synthesis of organic compounds via bio‐catalytic (green) approaches. The findings presented here are targeting at transesterification of fats and oils into corresponding alkyl esters applicable, e.g., as alternative fuel substitutes. High conversion rates coupled with hyperactivation effects as well as highly appealing reusability behavior indicate the practical benefits even for technical applications. Conversion of lipids into derivatives by CLEAs as demonstrated here, might extend utilization and conversion possibilities of biomass.
format Article in Journal/Newspaper
author Schroeck, Andrea Maria
Schober, Sigurd
Mittelbach, Martin
spellingShingle Schroeck, Andrea Maria
Schober, Sigurd
Mittelbach, Martin
Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B
author_facet Schroeck, Andrea Maria
Schober, Sigurd
Mittelbach, Martin
author_sort Schroeck, Andrea Maria
title Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B
title_short Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B
title_full Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B
title_fullStr Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B
title_full_unstemmed Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B
title_sort highly active biocatalyst for transesterification: cross linked enzyme aggregates of thermomyces lanuginosus and candida antarctica b
publisher Wiley
publishDate 2013
url http://dx.doi.org/10.1002/ejlt.201300015
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fejlt.201300015
https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejlt.201300015
https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ejlt.201300015
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source European Journal of Lipid Science and Technology
volume 115, issue 10, page 1164-1172
ISSN 1438-7697 1438-9312
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/ejlt.201300015
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