True ileal amino acid digestibility and digestible indispensable amino acid scores (DIAASs) of plant-based protein foods.

Plant-based protein foods are increasingly common, but data on their nutritional protein quality are scarce. This study evaluated it for seitan (wheat-based food), tofu (soya-based food), soya milk, and a pea emulsion. The true ileal digestibility (TID) of their amino acids was determined in minipigs, to calculate the digestible indispensable amino acid score (DIAAS). The TID of the proteins was high and not significantly different between the foods tested: 97% for seitan, 95% for tofu, 92% for soya milk and 94% for pea emulsion. There were only minor differences in individual amino acid TIDs. DIAAS ranking was thus essentially driven by the amino acid composition of the food: soya-based food > pea emulsion > seitan. Nevertheless, the lower TID of sulphur-containing amino acids in tofu than in soya milk induced a significant decrease in DIAAS (from 117% to 97%), highlighting the importance of the matrix effect on nutritional protein quality.

Food-dependent set-up of the DiDGI® dynamic in vitro system: Correlation with the porcine model for protein digestion of soya-based food.

The present study compared in vivo protein digestion in a miniature pig model with the dynamic in vitro system DiDGI®, using three digestive compartments (stomach, duodenum, and jejunum + ileum). Two soya-based meals-commercial soya milk and tofu-were studied, each with the same macronutrient content but different macrostructures. Our aim was to first deduce from the in vivo experiments in pigs key digestive parameters such as gastric pH, stomach emptying kinetics, and intestinal transit time, in order to design a relevant set-up for the dynamic in vitro system. Then, we compared digestive samples collected at fixed sampling times from both in vivo and in vitro models regarding different values related to proteolysis. We observed similar evolutions of gastric peptide distribution and duodenal proteolysis between models. Overall, apparent ileal digestibility of nitrogen was similar in vitro and in vivo and the differences between the two meals were conserved between models.

Hydrolysis of plant proteins at the molecular and supra-molecular scales during in vitro digestion.

The digestion of plant protein is highly dependent on multiple factors, with two of the most important being the protein source and the food matrix. The present study investigated the effects of these two factors on the digestion of seitan (a wheat-based food), tofu, soya juice, and a homemade emulsion of soy oil and water that was stabilised with pea protein. The four plant matrices and their respective protein isolates/concentrates (wheat gluten, soya protein, pea protein) were subjected to in vitro static digestion following the INFOGEST consensus protocol. We monitored the release of α-amino groups during digestion. We found that food matrix had a strong influence on protein digestion: soya juice was more hydrolysed than fresh tofu (51.1% versus 33.1%; P = 0.0087), but fresh tofu was more hydrolysed than soya protein isolate (33.1% versus 17.9%; P < 0.0001). Likewise, the pea-protein emulsion was better hydrolysed than the pea-protein isolate (P = 0.0033). Differences were also detected between the two solid foods investigated here: a higher degree of hydrolysis was found for tofu compared to seitan (33.1% versus 11.8%), which was perhaps a function of the presence of numerous dense protein aggregates in the latter but not the former. Furthermore, freeze-drying more than doubled the final degree of hydrolysis of seitan (P < 0.0001), but had no effect on tofu (P = 1.0000). Confocal microscopy revealed that protein networks in freeze-dried seitan were strongly altered with respect to the fresh product; instead, protein networks in freeze-dried and fresh tofu were largely similar. Finally, we found that the protease:protein ratio had a strong effect on the kinetics of proteolysis: a 3.7-fold increase in the concentration of the soya protein isolate with respect to that of the soya juice decreased the final degree of hydrolysis from 50.3 to 17.9% (P = 0.0988).

Temporal changes in postprandial intragastric pH: Comparing measurement methods, food structure effects, and kinetic modelling.

Intragastric pH greatly affects food disintegration and the release of nutrients in the gut. Here, the behaviour of two liquid meals (soymilk, pea emulsion) and two solid meals (tofu, seitan) was tested in miniature pigs fitted with gastric cannula. For 5 h, intragastric pH was recorded using one of three methods: ex vivo measurements of chyme samples, in situ measurements using pH catheters, or in situ measurements using wireless pH capsules, both inserted through a pig's cannula. The pH values obtained with the two in situ methods were highly correlated. The liquid and solid foods yielded distinct pH kinetics. For the solids, pH simply decreased exponentially. For the liquids, pH increased rapidly and then plateaued for 2 h before dropping Food macrostructure and, to a lesser extent, food buffering capacity clearly had an impact on intragastric pH. We modelled changes in intragastric pH over time with food-dependent nonlinear equations.

The chemical coding of 5-hydroxytryptamine containing enteroendocrine cells in the mouse gastrointestinal tract.

The majority of 5-HT (serotonin) in the body is contained in enteroendocrine cells of the gastrointestinal mucosa. From the time of their discovery over 80 years ago, the 5-HT-containing cells have been regarded as a class of cell that is distinct from enteroendocrine cells that contain peptide hormones. However, recent studies have cast doubt on the concept of there being distinct classes of enteroendocrine cells, each containing a single hormone or occasionally more than one hormone. Instead, data are rapidly accumulating that there are complex patterns of colocalisation of hormones that identify multiple subclasses of enteroendocrine cells. In the present work, multiple labelling immunohistochemistry is used to investigate patterns of colocalisation of 5-HT with enteric peptide hormones. Over 95 % of 5-HT cells in the duodenum also contained cholecystokinin and about 40 % of them also contained secretin. In the jejunum, about 75 % of 5-HT cells contained cholecystokinin but not secretin and 25 % contained 5-HT plus both cholecystokinin and secretin. Small proportions of 5-HT cells contained gastrin or somatostatin in the stomach, PYY or GLP-1 in the small intestine and GLP-1 or somatostatin in the large intestine. Rare or very rare 5-HT cells contained ghrelin (stomach), neurotensin (small and large intestines), somatostatin (small intestine) and PYY (in the large intestine). It is concluded that 5-HT-containing enteroendocrine cells are heterogeneous in their chemical coding and by implication in their functions.