Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis
The reaction kinetics of Candida antarctica lipase B (CalB) in the commercially available preparation Novozym (R) 435 (N435) were compared to those of preparations of CalB immobilised on Accurel (R) MP1000 (porous polypropylene). Two polypropylene preparations were made using enzyme loadings of 0.2%...
Published in: | Biocatalysis and Biotransformation |
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Language: | English |
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Taylor & Francis
2013
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Online Access: | https://lup.lub.lu.se/record/4170425 https://doi.org/10.3109/10242422.2013.837240 |
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ftulundlup:oai:lup.lub.lu.se:51306725-40ff-4587-8b7d-549905a6ae35 2023-05-15T13:35:34+02:00 Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis Nordblad, Mathias Adlercreutz, Patrick 2013 https://lup.lub.lu.se/record/4170425 https://doi.org/10.3109/10242422.2013.837240 eng eng Taylor & Francis https://lup.lub.lu.se/record/4170425 http://dx.doi.org/10.3109/10242422.2013.837240 wos:000325814900002 scopus:84885929452 Biocatalysis and Biotransformation; 31(5), pp 237-245 (2013) ISSN: 1024-2422 Industrial Biotechnology Lipase immobilisation enzyme kinetics acrylation contributiontojournal/article info:eu-repo/semantics/article text 2013 ftulundlup https://doi.org/10.3109/10242422.2013.837240 2023-02-01T23:29:14Z The reaction kinetics of Candida antarctica lipase B (CalB) in the commercially available preparation Novozym (R) 435 (N435) were compared to those of preparations of CalB immobilised on Accurel (R) MP1000 (porous polypropylene). Two polypropylene preparations were made using enzyme loadings of 0.2% and 2% (w/w). All three preparations were used in hydrolysis as well as transesterification of two substrates, ethyl acrylate and ethyl methacrylate with octanol. Reactions carried out at water activity levels from 0.06 to 0.96 and at octanol concentrations between 25 and 500 mM showed that both water and octanol can inhibit CalB. Pronounced mass transfer limitations were also observed, which were more pronounced for N435 than for the two MP1000 preparations. The MP1000 preparations could thus use the lipase more efficiently in these reactions, achieving a specific activity (per g enzyme) between 5 and 20 times that of N435. To achieve high rates in the transesterification reaction, it is recommended to use low water activity and moderate alcohol concentration. In order to carry out a hydrolysis reaction, an intermediate water activity should be used to balance the effects of water as a limiting substrate and as a competitive inhibitor. Article in Journal/Newspaper Antarc* Antarctica Lund University Publications (LUP) Biocatalysis and Biotransformation 31 5 237 245 |
institution |
Open Polar |
collection |
Lund University Publications (LUP) |
op_collection_id |
ftulundlup |
language |
English |
topic |
Industrial Biotechnology Lipase immobilisation enzyme kinetics acrylation |
spellingShingle |
Industrial Biotechnology Lipase immobilisation enzyme kinetics acrylation Nordblad, Mathias Adlercreutz, Patrick Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis |
topic_facet |
Industrial Biotechnology Lipase immobilisation enzyme kinetics acrylation |
description |
The reaction kinetics of Candida antarctica lipase B (CalB) in the commercially available preparation Novozym (R) 435 (N435) were compared to those of preparations of CalB immobilised on Accurel (R) MP1000 (porous polypropylene). Two polypropylene preparations were made using enzyme loadings of 0.2% and 2% (w/w). All three preparations were used in hydrolysis as well as transesterification of two substrates, ethyl acrylate and ethyl methacrylate with octanol. Reactions carried out at water activity levels from 0.06 to 0.96 and at octanol concentrations between 25 and 500 mM showed that both water and octanol can inhibit CalB. Pronounced mass transfer limitations were also observed, which were more pronounced for N435 than for the two MP1000 preparations. The MP1000 preparations could thus use the lipase more efficiently in these reactions, achieving a specific activity (per g enzyme) between 5 and 20 times that of N435. To achieve high rates in the transesterification reaction, it is recommended to use low water activity and moderate alcohol concentration. In order to carry out a hydrolysis reaction, an intermediate water activity should be used to balance the effects of water as a limiting substrate and as a competitive inhibitor. |
format |
Article in Journal/Newspaper |
author |
Nordblad, Mathias Adlercreutz, Patrick |
author_facet |
Nordblad, Mathias Adlercreutz, Patrick |
author_sort |
Nordblad, Mathias |
title |
Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis |
title_short |
Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis |
title_full |
Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis |
title_fullStr |
Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis |
title_full_unstemmed |
Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis |
title_sort |
immobilisation procedure and reaction conditions for optimal performance of candida antarctica lipase b in transesterification and hydrolysis |
publisher |
Taylor & Francis |
publishDate |
2013 |
url |
https://lup.lub.lu.se/record/4170425 https://doi.org/10.3109/10242422.2013.837240 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biocatalysis and Biotransformation; 31(5), pp 237-245 (2013) ISSN: 1024-2422 |
op_relation |
https://lup.lub.lu.se/record/4170425 http://dx.doi.org/10.3109/10242422.2013.837240 wos:000325814900002 scopus:84885929452 |
op_doi |
https://doi.org/10.3109/10242422.2013.837240 |
container_title |
Biocatalysis and Biotransformation |
container_volume |
31 |
container_issue |
5 |
container_start_page |
237 |
op_container_end_page |
245 |
_version_ |
1766067251227656192 |