Enzymatic fatty acid exchange in digalactosyldiacylglycerol
Persson, Mattias ; Svensson, Ingemar LU and Adlercreutz, Patrick LU
(2000)
In Chemistry and Physics of Lipids
104(1).
p.13-21
- Abstract
Six different lipases were screened for their ability of acidolysis between digalactosyldiacylglycerol (DGDG) and heptadecanoic acid in toluene. Lipases from Geotrichum candidum, Alcaligenes sp. and Penicillium camembertii did not catalyse the acidolysis reaction. Rhizopus arrhizus and Rhizomucor miehei (Lipozyme) catalysed the acidolysis but produced a mixture of DGMG, DGDG, acyl-DGMG and acyl-DGDG. The extra acyl group is bound to the primary hydroxyl of the digalactosyl moiety. Candida antarctica also catalysed the acidolysis but the TLC analysis showed bands with higher R(f) values than acyl-DGDG, these probably being different tetra and higher esters. R. arrhizus lipase was the most promising enzyme under the conditions used, with... (More)
Six different lipases were screened for their ability of acidolysis between digalactosyldiacylglycerol (DGDG) and heptadecanoic acid in toluene. Lipases from Geotrichum candidum, Alcaligenes sp. and Penicillium camembertii did not catalyse the acidolysis reaction. Rhizopus arrhizus and Rhizomucor miehei (Lipozyme) catalysed the acidolysis but produced a mixture of DGMG, DGDG, acyl-DGMG and acyl-DGDG. The extra acyl group is bound to the primary hydroxyl of the digalactosyl moiety. Candida antarctica also catalysed the acidolysis but the TLC analysis showed bands with higher R(f) values than acyl-DGDG, these probably being different tetra and higher esters. R. arrhizus lipase was the most promising enzyme under the conditions used, with no tetra esters being formed and giving the highest reaction rate of the enzymes investigated. Low water activity (0.06 or 0.11) and high fatty acid concentration (400 mM) increased the formation of acyl-DGDG whilst higher water activities (0.33 and 0.54) increased the amount of DGMG when R. arrhizus lipase was used as catalyst. At a water activity of 0.11 and a fatty acid concentration of 400 mM a yield of 24% modified DGDG was obtained. In this product the fatty acid originally present in the sn-1 position had been exchanged by heptadecanoic acid. Copyright (C) 2000 Elsevier Science Ireland Ltd.
(Less)
- author
- Persson, Mattias
; Svensson, Ingemar
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2000-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Digalactosyldiacylglycerol, Galactolipid, Lipase, Lipid modification
- in
- Chemistry and Physics of Lipids
- volume
- 104
- issue
- 1
- pages
- 9 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0033991426
- pmid:10660208
- ISSN
- 0009-3084
- DOI
- 10.1016/S0009-3084(99)00099-7
- language
- English
- LU publication?
- yes
- id
- 6e739c05-2c8e-43bb-9847-f808fe7e62f1
- date added to LUP
- 2019-06-20 15:57:28
- date last changed
- 2024-04-02 10:56:16
@article{6e739c05-2c8e-43bb-9847-f808fe7e62f1,
abstract = {{<p>Six different lipases were screened for their ability of acidolysis between digalactosyldiacylglycerol (DGDG) and heptadecanoic acid in toluene. Lipases from Geotrichum candidum, Alcaligenes sp. and Penicillium camembertii did not catalyse the acidolysis reaction. Rhizopus arrhizus and Rhizomucor miehei (Lipozyme) catalysed the acidolysis but produced a mixture of DGMG, DGDG, acyl-DGMG and acyl-DGDG. The extra acyl group is bound to the primary hydroxyl of the digalactosyl moiety. Candida antarctica also catalysed the acidolysis but the TLC analysis showed bands with higher R(f) values than acyl-DGDG, these probably being different tetra and higher esters. R. arrhizus lipase was the most promising enzyme under the conditions used, with no tetra esters being formed and giving the highest reaction rate of the enzymes investigated. Low water activity (0.06 or 0.11) and high fatty acid concentration (400 mM) increased the formation of acyl-DGDG whilst higher water activities (0.33 and 0.54) increased the amount of DGMG when R. arrhizus lipase was used as catalyst. At a water activity of 0.11 and a fatty acid concentration of 400 mM a yield of 24% modified DGDG was obtained. In this product the fatty acid originally present in the sn-1 position had been exchanged by heptadecanoic acid. Copyright (C) 2000 Elsevier Science Ireland Ltd.</p>}},
author = {{Persson, Mattias and Svensson, Ingemar and Adlercreutz, Patrick}},
issn = {{0009-3084}},
keywords = {{Digalactosyldiacylglycerol; Galactolipid; Lipase; Lipid modification}},
language = {{eng}},
month = {{01}},
number = {{1}},
pages = {{13--21}},
publisher = {{Elsevier}},
series = {{Chemistry and Physics of Lipids}},
title = {{Enzymatic fatty acid exchange in digalactosyldiacylglycerol}},
url = {{http://dx.doi.org/10.1016/S0009-3084(99)00099-7}},
doi = {{10.1016/S0009-3084(99)00099-7}},
volume = {{104}},
year = {{2000}},
}