Interesterification of phosphatidylcholine with lipases in organic media
Svensson, Ingemar LU ; Adlercreutz, Patrick LU
and Mattiasson, Bo
LU
(1990)
In Applied Microbiology and Biotechnology
33(3).
p.255-258
- Abstract
Lipases were investigated with respect to their ability to catalyse the incorporation of fatty acids into phosphatidylcholine (PC) by interesterification reactions. The enzymes were dried onto solid support materials and the conversions were carried out in water-saturated toluene. Three lipases (two fungal and one plant enzyme) had the desired activity; immobilized lipase from Mucor miehei (Lipozyme) was the most active enzyme. The Lipozyme-catalysed interesterification was selective for the sn-1 position of PC and during 48 h of reaction around 50% of the fatty acids in this position were replaced with heptadecanoic acid, a fatty acid which was practically absent in the original phospholipid. Due to adsorption on the support material... (More)
Lipases were investigated with respect to their ability to catalyse the incorporation of fatty acids into phosphatidylcholine (PC) by interesterification reactions. The enzymes were dried onto solid support materials and the conversions were carried out in water-saturated toluene. Three lipases (two fungal and one plant enzyme) had the desired activity; immobilized lipase from Mucor miehei (Lipozyme) was the most active enzyme. The Lipozyme-catalysed interesterification was selective for the sn-1 position of PC and during 48 h of reaction around 50% of the fatty acids in this position were replaced with heptadecanoic acid, a fatty acid which was practically absent in the original phospholipid. Due to adsorption on the support material and the competing hydrolysis reaction the total amount of PC in the reaction solution decreased to about 40% of the original amount. Higher interesterification rates were obtained with free fatty acids as acyl donors than with fatty acid esters.
(Less)
- author
- Svensson, Ingemar
LU
; Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1990
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Applied Microbiology and Biotechnology
- volume
- 33
- issue
- 3
- pages
- 255 - 258
- publisher
- Springer
- external identifiers
-
- pmid:1366637
- scopus:0025037298
- ISSN
- 0175-7598
- DOI
- 10.1007/BF00164517
- language
- English
- LU publication?
- yes
- id
- 23579bf4-74b6-4566-80b4-d15324624f15
- date added to LUP
- 2019-06-20 15:44:49
- date last changed
- 2024-04-02 09:07:43
@article{23579bf4-74b6-4566-80b4-d15324624f15,
abstract = {{<p>Lipases were investigated with respect to their ability to catalyse the incorporation of fatty acids into phosphatidylcholine (PC) by interesterification reactions. The enzymes were dried onto solid support materials and the conversions were carried out in water-saturated toluene. Three lipases (two fungal and one plant enzyme) had the desired activity; immobilized lipase from Mucor miehei (Lipozyme) was the most active enzyme. The Lipozyme-catalysed interesterification was selective for the sn-1 position of PC and during 48 h of reaction around 50% of the fatty acids in this position were replaced with heptadecanoic acid, a fatty acid which was practically absent in the original phospholipid. Due to adsorption on the support material and the competing hydrolysis reaction the total amount of PC in the reaction solution decreased to about 40% of the original amount. Higher interesterification rates were obtained with free fatty acids as acyl donors than with fatty acid esters.</p>}},
author = {{Svensson, Ingemar and Adlercreutz, Patrick and Mattiasson, Bo}},
issn = {{0175-7598}},
language = {{eng}},
number = {{3}},
pages = {{255--258}},
publisher = {{Springer}},
series = {{Applied Microbiology and Biotechnology}},
title = {{Interesterification of phosphatidylcholine with lipases in organic media}},
url = {{http://dx.doi.org/10.1007/BF00164517}},
doi = {{10.1007/BF00164517}},
volume = {{33}},
year = {{1990}},
}