![]() (7) In a previous study by Blom et al., (8) mean gastric ghrelin release was reduced by 46% after intake of a high-protein diet (58.1% of energy from protein and 14.1% of energy from carbohydrate) as compared to a high-carbohydrate diet (19.3% of energy from protein and 47.3% of energy from carbohydrate). This resulted in a reduction of the mean proton secretion promoted by the peptides by up to 86.3 ± 9.9% for TAS2R16kd ( p < 0.0001) cells and by up to 62.8 ± 7.0% for TAS2R38kd ( p < 0.0001) cells compared with mock-transfected cells.īesides the effects on hormones promoting satiation, a reduction of food intake by dietary proteins can also be achieved by regulation of the so-called “hunger hormone” ghrelin, which promotes the feeling of hunger. The functional involvement of these TAS2Rs was verified by siRNA knock-down (kd) experiments in HGT-1 cells. For three of these peptides (YFYPEL, VAPFPEVF, and YQEPVLGPVRGPFPIIV), an upregulation of gene expression of TAS2R16 and TAS2R38 was observed. The bitterness of five selected casein-derived peptides was validated by sensory analyses and by an in vitro screening approach based on human gastric parietal cells (HGT-1). An in vitro model of gastric digestion was verified by casein-fed pigs, and the peptides resulting from gastric digestion were identified by liquid chromatography–time-of-flight-mass spectrometry. Here, we tried to elucidate whether dietary non-bitter-tasting casein is intra-gastrically degraded into bitter peptides that stimulate mechanisms of gastric acid secretion in physiologically achievable concentrations. ![]() ![]() ![]() Previous studies of our group demonstrated that bitter-tasting food constituents, such as caffeine, stimulate mechanisms of gastric acid secretion as a signal of gastric satiation and a key process of gastric protein digestion via activation of bitter taste receptors (TAS2Rs). Eating satiating, protein-rich foods is one of the key aspects of modern diet, although a bitter off-taste often limits the application of some proteins and protein hydrolysates, especially in processed foods. ![]()
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