New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB

Abstract Candida antartica lipase B (CALB) is the most versatile biocatalyst and is, therefore, widely used in industry. Its advantages range from thermostability, stereoselectivity, and activity in organic solvents to the acceptance of nucleophiles other than water. The actual standard for industri...

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Published in:European Journal of Lipid Science and Technology
Main Authors: Basso, Alessandra, Froment, Luc, Hesseler, Martin, Serban, Simona
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2013
Subjects:
Online Access:http://dx.doi.org/10.1002/ejlt.201200419
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spelling crwiley:10.1002/ejlt.201200419 2024-06-23T07:48:04+00:00 New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB Basso, Alessandra Froment, Luc Hesseler, Martin Serban, Simona 2013 http://dx.doi.org/10.1002/ejlt.201200419 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fejlt.201200419 https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejlt.201200419 https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ejlt.201200419 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Lipid Science and Technology volume 115, issue 4, page 468-472 ISSN 1438-7697 1438-9312 journal-article 2013 crwiley https://doi.org/10.1002/ejlt.201200419 2024-06-04T06:45:01Z Abstract Candida antartica lipase B (CALB) is the most versatile biocatalyst and is, therefore, widely used in industry. Its advantages range from thermostability, stereoselectivity, and activity in organic solvents to the acceptance of nucleophiles other than water. The actual standard for industrial applications of CALB is the immobilized enzyme on Lewatit VP OC 1600 and is marketed under the name Novozym® 435. A new acrylic enzyme carrier (ECR1030) for the immobilization by adsorption of CALB and for use in batch or column reactors has been developed. The resin shows an activity of >9000 PLU/g Dry , which is similar to Novozym® 435. Protein loading was 24.4 mg/g Wet, and immobilizations yields higher than 90% were obtained. Unlike the resin used for the production of Novozym® 435, ECR1030 possesses high mechanical stability and is therefore more suitable for applications that expose the polymers to high mechanical stress, such as multiple reuses in stirred reactors. Practical applications: Immobilized CALB is the biocatalyst used in the widest amount of industrial applications due to its broad selectivity and stability. It can be used for the manufacture of specialty chemicals such as surfactants, amides, chiral amines, alcohols, biodiesel, and polyesters. Its industrial use is in stirred tanks or packed columns, so high mechanical stability is needed together with high activity and sustainable costs. Article in Journal/Newspaper antartic* Wiley Online Library European Journal of Lipid Science and Technology 115 4 468 472
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract Candida antartica lipase B (CALB) is the most versatile biocatalyst and is, therefore, widely used in industry. Its advantages range from thermostability, stereoselectivity, and activity in organic solvents to the acceptance of nucleophiles other than water. The actual standard for industrial applications of CALB is the immobilized enzyme on Lewatit VP OC 1600 and is marketed under the name Novozym® 435. A new acrylic enzyme carrier (ECR1030) for the immobilization by adsorption of CALB and for use in batch or column reactors has been developed. The resin shows an activity of >9000 PLU/g Dry , which is similar to Novozym® 435. Protein loading was 24.4 mg/g Wet, and immobilizations yields higher than 90% were obtained. Unlike the resin used for the production of Novozym® 435, ECR1030 possesses high mechanical stability and is therefore more suitable for applications that expose the polymers to high mechanical stress, such as multiple reuses in stirred reactors. Practical applications: Immobilized CALB is the biocatalyst used in the widest amount of industrial applications due to its broad selectivity and stability. It can be used for the manufacture of specialty chemicals such as surfactants, amides, chiral amines, alcohols, biodiesel, and polyesters. Its industrial use is in stirred tanks or packed columns, so high mechanical stability is needed together with high activity and sustainable costs.
format Article in Journal/Newspaper
author Basso, Alessandra
Froment, Luc
Hesseler, Martin
Serban, Simona
spellingShingle Basso, Alessandra
Froment, Luc
Hesseler, Martin
Serban, Simona
New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
author_facet Basso, Alessandra
Froment, Luc
Hesseler, Martin
Serban, Simona
author_sort Basso, Alessandra
title New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
title_short New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
title_full New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
title_fullStr New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
title_full_unstemmed New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
title_sort new highly robust divinyl benzene/acrylate polymer for immobilization of lipase calb
publisher Wiley
publishDate 2013
url http://dx.doi.org/10.1002/ejlt.201200419
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fejlt.201200419
https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejlt.201200419
https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ejlt.201200419
genre antartic*
genre_facet antartic*
op_source European Journal of Lipid Science and Technology
volume 115, issue 4, page 468-472
ISSN 1438-7697 1438-9312
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/ejlt.201200419
container_title European Journal of Lipid Science and Technology
container_volume 115
container_issue 4
container_start_page 468
op_container_end_page 472
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