Digestion of triacylgycerols containing longchain polyenoic fatty acids in vitro by colipase dependent lipase and human milk bile salt stimulated lipase
(1994) In Biochimica et Biophysica Acta 121(2). p.239-243- Abstract
- To assess the role of human milk bile salt-stimulated lipase (BSSL) in the digestion of polyunsaturated ester bonds of triacylglycerols, hydrolysis of docosahexaenoic acid (22:6(n − 3)) ester bonds was compared to that of oleic acid (18:1(n − 9)) or arachidonic acid (20:4(n − 6)) esters. As model substrates, we used rat chylomicrons obtained after feeding human milk fat globules and radiolabeled fatty acids. Radiolabeled chylomicrons were incubated with colipase-dependent pancreatic lipase, with BSSL, or with both enzymes in combination. Both enzymes hydrolyzed 18:1 more efficiently than 22:6 esters. With colipase-dependent lipase there was a large accumulation of 22:6 in diacylglycerol whereas with BSSL it accumulated mainly in... (More)
- To assess the role of human milk bile salt-stimulated lipase (BSSL) in the digestion of polyunsaturated ester bonds of triacylglycerols, hydrolysis of docosahexaenoic acid (22:6(n − 3)) ester bonds was compared to that of oleic acid (18:1(n − 9)) or arachidonic acid (20:4(n − 6)) esters. As model substrates, we used rat chylomicrons obtained after feeding human milk fat globules and radiolabeled fatty acids. Radiolabeled chylomicrons were incubated with colipase-dependent pancreatic lipase, with BSSL, or with both enzymes in combination. Both enzymes hydrolyzed 18:1 more efficiently than 22:6 esters. With colipase-dependent lipase there was a large accumulation of 22:6 in diacylglycerol whereas with BSSL it accumulated mainly in monoacylglycerol. Esters containing 20:4 were hydrolyzed by BSSL as efficiently as 18:1 but this fatty acid also accumulated as diacylglycerol with colipase-dependent lipase. At low bile salt concentrations, as found in duodenal contents of newborns, colipase-dependent lipase was virtually unable to hydrolyze esters of 20:4 and 22:6 whereas BSSL hydrolyzed these esters at appreciable rates. Combining the two enzymes gave the most efficient hydrolysis of all fatty acids tested regardless of bile salt concentrations. BSSL may thus have a physiological role in completing duodenal hydrolysis of milk triacylglycerols containing 22:6- or 20:4-esters to free fatty acids and monoacylglycerol. (Less)
- Abstract (Swedish)
- To assess the role of human milk bile salt-stimulated lipase (BSSL) in the digestion of polyunsaturated ester bonds of triacylglycerols, hydrolysis of docosahexaenoic acid (22:6(n-3)) ester bonds was compared to that of oleic acid (18:1(n-9)) or arachidonic acid (20:4(n-6)) esters. As model substrates, we used rat chylomicrons obtained after feeding human milk fat globules and radiolabeled fatty acids. Radiolabeled chylomicrons were incubated with colipase-dependent pancreatic lipase, with BSSL, or with both enzymes in combination. Both enzymes hydrolyzed 18:1 more efficiently than 22:6 esters. With colipase-dependent lipase there was a large accumulation of 22:6 in diacylglycerol whereas with BSSL it accumulated mainly in... (More)
- To assess the role of human milk bile salt-stimulated lipase (BSSL) in the digestion of polyunsaturated ester bonds of triacylglycerols, hydrolysis of docosahexaenoic acid (22:6(n-3)) ester bonds was compared to that of oleic acid (18:1(n-9)) or arachidonic acid (20:4(n-6)) esters. As model substrates, we used rat chylomicrons obtained after feeding human milk fat globules and radiolabeled fatty acids. Radiolabeled chylomicrons were incubated with colipase-dependent pancreatic lipase, with BSSL, or with both enzymes in combination. Both enzymes hydrolyzed 18:1 more efficiently than 22:6 esters. With colipase-dependent lipase there was a large accumulation of 22:6 in diacylglycerol whereas with BSSL it accumulated mainly in monoacylglycerol. Esters containing 20:4 were hydrolyzed by BSSL as efficiently as 18:1 but this fatty acid also accumulated as diacylglycerol with colipase-dependent lipase. At low bile salt concentrations, as found in duodenal contents of newborns, colipase-dependent lipase was virtually unable to hydrolyze esters of 20:4 and 22:6 whereas BSSL hydrolyzed these esters at appreciable rates. Combining the two enzymes gave the most efficient hydrolysis of all fatty acids tested regardless of bile salt concentrations. BSSL may thus have a physiological role in completing duodenal hydrolysis of milk triacylglycerols containing 22:6- or 20:4-esters to free fatty acids and monoacylglycerol. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3835e1a4-29e2-4094-9ffa-9c59020de50d
- author
- Chen, Qi ; Bläckberg, Lars ; Nilsson, Åke LU ; Sternby, Berit LU and Hernell, Olle
- organization
- publishing date
- 1994-01-03
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochimica et Biophysica Acta
- volume
- 121
- issue
- 2
- pages
- 239 - 243
- publisher
- Elsevier
- external identifiers
-
- scopus:0028013634
- ISSN
- 0006-3002
- DOI
- 10.1016/0005-2760(94)90127-9
- language
- English
- LU publication?
- yes
- id
- 3835e1a4-29e2-4094-9ffa-9c59020de50d
- date added to LUP
- 2019-06-20 17:18:15
- date last changed
- 2024-01-01 12:09:26
@article{3835e1a4-29e2-4094-9ffa-9c59020de50d,
abstract = {{To assess the role of human milk bile salt-stimulated lipase (BSSL) in the digestion of polyunsaturated ester bonds of triacylglycerols, hydrolysis of docosahexaenoic acid (22:6(n − 3)) ester bonds was compared to that of oleic acid (18:1(n − 9)) or arachidonic acid (20:4(n − 6)) esters. As model substrates, we used rat chylomicrons obtained after feeding human milk fat globules and radiolabeled fatty acids. Radiolabeled chylomicrons were incubated with colipase-dependent pancreatic lipase, with BSSL, or with both enzymes in combination. Both enzymes hydrolyzed 18:1 more efficiently than 22:6 esters. With colipase-dependent lipase there was a large accumulation of 22:6 in diacylglycerol whereas with BSSL it accumulated mainly in monoacylglycerol. Esters containing 20:4 were hydrolyzed by BSSL as efficiently as 18:1 but this fatty acid also accumulated as diacylglycerol with colipase-dependent lipase. At low bile salt concentrations, as found in duodenal contents of newborns, colipase-dependent lipase was virtually unable to hydrolyze esters of 20:4 and 22:6 whereas BSSL hydrolyzed these esters at appreciable rates. Combining the two enzymes gave the most efficient hydrolysis of all fatty acids tested regardless of bile salt concentrations. BSSL may thus have a physiological role in completing duodenal hydrolysis of milk triacylglycerols containing 22:6- or 20:4-esters to free fatty acids and monoacylglycerol.}},
author = {{Chen, Qi and Bläckberg, Lars and Nilsson, Åke and Sternby, Berit and Hernell, Olle}},
issn = {{0006-3002}},
language = {{eng}},
month = {{01}},
number = {{2}},
pages = {{239--243}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Digestion of triacylgycerols containing longchain polyenoic fatty acids in vitro by colipase dependent lipase and human milk bile salt stimulated lipase}},
url = {{http://dx.doi.org/10.1016/0005-2760(94)90127-9}},
doi = {{10.1016/0005-2760(94)90127-9}},
volume = {{121}},
year = {{1994}},
}