β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acids uptake
Author
Le Maux, SoleneBrodkorb, Andre

Croguennec, Thomas
Hennessy, Alan A.
Bouhallab, Said
Giblin, Linda

Date
2013-07
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Le Maux, S., Brodkorb, A., Croguennec, T., Hennessy, A. A., Bouhallab, S., & Giblin, L. (2013). β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acids uptake. Journal of Dairy Science, 96(7), 4258-4268. doi: http://dx.doi.org/10.3168/jds.2013-6682Abstract
The dairy protein β-lactoglobulin (BLG) is known to bind fatty acids such as the salt of the essential longchain fatty acid linoleic acid (cis,cis-9,12-octadecadienoic acid, n-6, 18:2). The aim of the current study was to investigate how bovine BLG-linoleate complexes, of various stoichiometry, affect the enzymatic digestion of BLG and the intracellular transport of linoleate into enterocyte-like monolayers. Duodenal and gastric digestions of the complexes indicated that BLG was hydrolyzed more rapidly when complexed with linoleate. Digested as well as undigested BLG-linoleate complexes reduced intracellular linoleate transport as compared with free linoleate. To investigate whether enteroendocrine cells perceive linoleate differently when part of a complex, the ability of linoleate to increase production or secretion of the enteroendocrine satiety hormone, cholecystokinin, was measured. Cholecystokinin mRNA levels were different when linoleate was presented to the cells alone or as part of a protein complex. In conclusion, understanding interactions between linoleate and BLG could help to formulate foods with targeted fatty acid bioaccessibility and, therefore, aid in the development of food matrices with optimal bioactive efficacyFunder
Department of Agriculture, Food and the Marine; Irish Research Council for Science, Engineering and Technology; Teagasc Walsh Fellowship ProgrammeGrant Number
08/RD/TMFRC/650ae974a485f413a2113503eed53cd6c53
http://dx.doi.org/ 10.3168/jds.2013-6682