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Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis

Nordblad, Mathias LU and Adlercreutz, Patrick LU orcid (2013) In Biocatalysis and Biotransformation 31(5). p.237-245
Abstract
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... (More)
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. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Lipase immobilisation, enzyme kinetics, acrylation
in
Biocatalysis and Biotransformation
volume
31
issue
5
pages
237 - 245
publisher
Taylor & Francis
external identifiers
  • wos:000325814900002
  • scopus:84885929452
ISSN
1024-2422
DOI
10.3109/10242422.2013.837240
language
English
LU publication?
yes
id
51306725-40ff-4587-8b7d-549905a6ae35 (old id 4170425)
date added to LUP
2016-04-01 10:31:00
date last changed
2022-02-25 02:33:06
@article{51306725-40ff-4587-8b7d-549905a6ae35,
  abstract     = {{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.}},
  author       = {{Nordblad, Mathias and Adlercreutz, Patrick}},
  issn         = {{1024-2422}},
  keywords     = {{Lipase immobilisation; enzyme kinetics; acrylation}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{237--245}},
  publisher    = {{Taylor & Francis}},
  series       = {{Biocatalysis and Biotransformation}},
  title        = {{Immobilisation procedure and reaction conditions for optimal performance of Candida antarctica lipase B in transesterification and hydrolysis}},
  url          = {{http://dx.doi.org/10.3109/10242422.2013.837240}},
  doi          = {{10.3109/10242422.2013.837240}},
  volume       = {{31}},
  year         = {{2013}},
}