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Lipase-catalyzed transesterification of phosphatidylcholine at controlled water activity

Svensson, Ingemar LU ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1992) In Journal of the American Oil Chemists' Society 69(10). p.986-991
Abstract

The incorporation of a free fatty acid into the sn-1 position of phosphatidylcholine by lipase-catalyzed transesterification was investigated. The thermodynamic water activity of both the enzyme preparation and the substrate solution was adjusted to the same value prior to the reaction. The reaction rate increased with increasing water activity but the yield of modified phosphatidylcholine decreased due to hydrolysis. By using a large excess of the free fatty acid (heptadecanoic acid), the hydrolysis reaction was slowed down, so a higher yield was obtained at a given degree of incorporation. The best results were obtained with Rhizopus arrhizus lipase immobilized by adsorption on a polypropylene support. With this preparation, a yield... (More)

The incorporation of a free fatty acid into the sn-1 position of phosphatidylcholine by lipase-catalyzed transesterification was investigated. The thermodynamic water activity of both the enzyme preparation and the substrate solution was adjusted to the same value prior to the reaction. The reaction rate increased with increasing water activity but the yield of modified phosphatidylcholine decreased due to hydrolysis. By using a large excess of the free fatty acid (heptadecanoic acid), the hydrolysis reaction was slowed down, so a higher yield was obtained at a given degree of incorporation. The best results were obtained with Rhizopus arrhizus lipase immobilized by adsorption on a polypropylene support. With this preparation, a yield of 60% and nearly 50% incorporation of heptadecanoic acid (100% incorporation in the sn-1 position) was obtained at a water activity of 0.064. The enzyme preparation had good operational stability and position specificity. Little incorporation (<1%) was observed in the sn-2 position, when almost all the fatty acid in the sn-1 position was exchanged.

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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Lipase, phosphatidylcholine, transesterification, water activity
in
Journal of the American Oil Chemists' Society
volume
69
issue
10
pages
6 pages
publisher
The American Oil Chemists' Society
external identifiers
  • scopus:51249167282
ISSN
0003-021X
DOI
10.1007/BF02541063
language
English
LU publication?
yes
id
64abc2a2-a159-4914-b310-83cfd017a62b
date added to LUP
2019-06-22 09:24:30
date last changed
2021-06-27 06:04:08
@article{64abc2a2-a159-4914-b310-83cfd017a62b,
  abstract     = {{<p>The incorporation of a free fatty acid into the sn-1 position of phosphatidylcholine by lipase-catalyzed transesterification was investigated. The thermodynamic water activity of both the enzyme preparation and the substrate solution was adjusted to the same value prior to the reaction. The reaction rate increased with increasing water activity but the yield of modified phosphatidylcholine decreased due to hydrolysis. By using a large excess of the free fatty acid (heptadecanoic acid), the hydrolysis reaction was slowed down, so a higher yield was obtained at a given degree of incorporation. The best results were obtained with Rhizopus arrhizus lipase immobilized by adsorption on a polypropylene support. With this preparation, a yield of 60% and nearly 50% incorporation of heptadecanoic acid (100% incorporation in the sn-1 position) was obtained at a water activity of 0.064. The enzyme preparation had good operational stability and position specificity. Little incorporation (&lt;1%) was observed in the sn-2 position, when almost all the fatty acid in the sn-1 position was exchanged.</p>}},
  author       = {{Svensson, Ingemar and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0003-021X}},
  keywords     = {{Lipase; phosphatidylcholine; transesterification; water activity}},
  language     = {{eng}},
  month        = {{10}},
  number       = {{10}},
  pages        = {{986--991}},
  publisher    = {{The American Oil Chemists' Society}},
  series       = {{Journal of the American Oil Chemists' Society}},
  title        = {{Lipase-catalyzed transesterification of phosphatidylcholine at controlled water activity}},
  url          = {{http://dx.doi.org/10.1007/BF02541063}},
  doi          = {{10.1007/BF02541063}},
  volume       = {{69}},
  year         = {{1992}},
}