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β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acids uptake
Le Maux, Solene Brodkorb, Andre Croguennec, Thomas Hennessy, Alan A. Bouhallab, Said Giblin, Linda
Le Maux, Solene
Brodkorb, Andre
Croguennec, Thomas
Hennessy, Alan A.
Bouhallab, Said
Giblin, Linda
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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.2013-6682
Abstract
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 efficacy