Browsing Food Chemistry & Technology by Subject "Bioaccessibility"
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In vitro digestion of protein-enriched restructured beef steaks with pea protein isolate, rice protein and lentil flour following sous vide processingThe effect of plant protein inclusion in cooked meat upon in vitro gastro-intestinal (GI) digestion was investigated. Pea protein isolate, rice protein and lentil flour were used to increase the protein content in a meat model system restructured using two transglutaminase enzymes [Activa®EB (TG) and Transgluseen™-M (TS)]. Restructured beef steaks were subjected to simulated GI digestion using the static INFOGEST method. Samples taken at different digestion times were analysed using SDS-PAGE, size exclusion-HPLC, free amino acid analysis and microscopy. SDS-PAGE analysis revealed significant protein hydrolysis during GI digestion. Most soluble peptides had a molecular weight smaller than 500 Da, corresponding to peptides of <5 amino acids, regardless of food treatment. The amounts of released, free amino acids isoleucine, lysine, phenylalanine and valine were higher (P < 0.05) in lentil-enriched restructured beef steaks following GI digestion. Confocal laser scanning microscopy (CSLM) revealed pronounced aggregation in digested samples. In vitro digestates of protein-enriched restructured beef steaks showed lower production of small molecular weight peptides. This study demonstrated how the bioaccessibility of protein-enriched restructured beef steaks are influenced by formulation and processing.
β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acids uptakeThe 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