期刊
JOURNAL OF DAIRY SCIENCE
卷 96, 期 7, 页码 4258-4268出版社
ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2013-6682
关键词
beta-lactoglobulin; linoleate; in vitro digestion; bioaccessibility
资金
- Teagasc Walsh Fellowship
- Department of Agriculture, Fisheries and Food (Dublin, Ireland
- FIRM project) [08/RD/TMFRC/650]
- IRCSET-Ulysses Travel Grant (Dublin, Ireland)
The dairy protein beta-lactoglobulin (BLG) is known to bind fatty acids such as the salt of the essential long-chain 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据