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Please use this identifier to cite or link to this item: http://hdl.handle.net/11019/507

Title: β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acids uptake
Authors: Le Maux, Solene
Brodkorb, Andre
Croguennec, Thomas
Hennessy, Alan A
Bouhallab, Said
Giblin, Linda
Keywords: : β-lactoglobulin
In Vitro Digestion
Issue Date: Jul-2013
Publisher: Elsevier Inc and American Dairy Science Association
Citation: 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
Series/Report no.: Journal of Dairy Science;vol 96
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
Description: peer-reviewed
S. Le Maux is currently supported by a Teagasc Walsh Fellowship and the Department of Agriculture, Fisheries and Food (FIRM project 08/RD/TMFRC/650). We also acknowledge funding from IRCSET-Ulysses Travel Grant.
URI: http://hdl.handle.net/11019/507
http://dx.doi.org/ 10.3168/jds.2013-6682
Appears in Collections:Food Biosciences
Food Chemistry & Technology

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