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Adsorption of lipase on polypropylene powder

Gitlesen, Thomas ; Bauer, Michael and Adlercreutz, Patrick LU (1997) In Biochimica et Biophysica Acta - Lipids and Lipid Metabolism 1345(2). p.188-196
Abstract

Adsorption of different lipases by EP-100 polypropylene powder from pure and pure lipase preparations was studied. Langmuir isotherms described the adsorption equilibria well both for protein and lipase activity adsorption. Adsorption isotherms for five different proteins all gave a similar saturation level of 220 mg protein per g carrier. Twelve commercial lipase preparations were tested for selectivity in the adsorption of-lipase. For all preparations the selectivity factor was larger than one. In a crude lipase preparation from Pseudomonns fluorescence, the specific activity in solution decreased by two orders of magnitude after adsorption. The adsorption was not significantly influenced by pH changes in the adsorption buffer,... (More)

Adsorption of different lipases by EP-100 polypropylene powder from pure and pure lipase preparations was studied. Langmuir isotherms described the adsorption equilibria well both for protein and lipase activity adsorption. Adsorption isotherms for five different proteins all gave a similar saturation level of 220 mg protein per g carrier. Twelve commercial lipase preparations were tested for selectivity in the adsorption of-lipase. For all preparations the selectivity factor was larger than one. In a crude lipase preparation from Pseudomonns fluorescence, the specific activity in solution decreased by two orders of magnitude after adsorption. The adsorption was not significantly influenced by pH changes in the adsorption buffer, indicating that hydrophobic and not electrostatic interactions are the dominating adsorption forces. Adsorption of a crude lipase from Candida rugosa (Sigma) was fast and equilibrium was reached in 30 and 100 min for protein and lipase activity adsorption respectively. Desorption in aqueous solution wag negligible. Investigations with seven different lipases showed no correlation between the specific lipolytic activity of dissolved enzyme in aqueous solution and the specific activity of adsorbed enzyme in an esterification reaction in organic solvent.

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author
organization
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type
Contribution to journal
publication status
published
subject
keywords
Ajdsorption kinetics, Langmuir isotherm, Lipase adsorption
in
Biochimica et Biophysica Acta - Lipids and Lipid Metabolism
volume
1345
issue
2
pages
9 pages
publisher
Elsevier
external identifiers
  • pmid:9106498
  • scopus:0031127561
ISSN
0005-2760
DOI
10.1016/S0005-2760(96)00176-2
language
English
LU publication?
yes
id
4ac5b5ff-3f94-436c-821e-f68ba5388fd5
date added to LUP
2019-06-20 15:37:35
date last changed
2020-02-19 05:33:43
@article{4ac5b5ff-3f94-436c-821e-f68ba5388fd5,
  abstract     = {<p>Adsorption of different lipases by EP-100 polypropylene powder from pure and pure lipase preparations was studied. Langmuir isotherms described the adsorption equilibria well both for protein and lipase activity adsorption. Adsorption isotherms for five different proteins all gave a similar saturation level of 220 mg protein per g carrier. Twelve commercial lipase preparations were tested for selectivity in the adsorption of-lipase. For all preparations the selectivity factor was larger than one. In a crude lipase preparation from Pseudomonns fluorescence, the specific activity in solution decreased by two orders of magnitude after adsorption. The adsorption was not significantly influenced by pH changes in the adsorption buffer, indicating that hydrophobic and not electrostatic interactions are the dominating adsorption forces. Adsorption of a crude lipase from Candida rugosa (Sigma) was fast and equilibrium was reached in 30 and 100 min for protein and lipase activity adsorption respectively. Desorption in aqueous solution wag negligible. Investigations with seven different lipases showed no correlation between the specific lipolytic activity of dissolved enzyme in aqueous solution and the specific activity of adsorbed enzyme in an esterification reaction in organic solvent.</p>},
  author       = {Gitlesen, Thomas and Bauer, Michael and Adlercreutz, Patrick},
  issn         = {0005-2760},
  language     = {eng},
  month        = {04},
  number       = {2},
  pages        = {188--196},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Lipids and Lipid Metabolism},
  title        = {Adsorption of lipase on polypropylene powder},
  url          = {http://dx.doi.org/10.1016/S0005-2760(96)00176-2},
  doi          = {10.1016/S0005-2760(96)00176-2},
  volume       = {1345},
  year         = {1997},
}