Intestinal kinetics from digestion of milk proteins in humans

Objective. We aim to assess in humans the intestinal digestion of two protein fractions from milk, i.e. a soluble (SP) and non-soluble (casein; CAS) proteins, that exhibit opposite chemical and digestive characteristics

Earthworms Use Odor Cues to Locate and Feed on Microorganisms in Soil

Earthworms are key components of temperate soil ecosystems but key aspects of their ecology remain unexamined. Here we elucidate the role of olfactory cues in earthworm attraction to food sources and document specific chemical cues that attract Eisenia fetida to the soil fungi Geotrichum candidum. Fungi and other microorganisms are major sources of volatile emissions in soil ecosystems as well as primary food sources for earthworms, suggesting the likelihood that earthworms might profitably use olfactory cues to guide foraging behavior. Moreover, previous studies have documented earthworm movement toward microbial food sources. But, the specific olfactory cues responsible for earthworm attraction have not previously been identified. Using olfactometer assays combined with chemical analyses (GC-MS), we documented the attraction of E. fetida individuals to filtrate derived from G. candidum colonies and to two individual compounds tested in isolation: ethyl pentanoate and ethyl hexanoate. Attraction at a distance was observed when barriers prevented the worms from reaching the target stimuli, confirming the role of volatile cues. These findings enhance our understanding of the mechanisms underlying key trophic interactions in soil ecosystems and have potential implications for the extraction and collection of earthworms in vermiculture and other applied activities

Structural mechanism and kinetics of in vitro gastric digestion are affected by process-induced changes in bovine milk

Bovine milk is commonly exposed to processing, which can alter the structure, biochemical composition, physico-chemical properties and sensory quality. While many of these changes have been studied extensively, little is known about their effect on digestive behaviour. In this study, heat treatments of pasteurisation at 72 °C for 15 s or Ultra-High-Temperature (UHT) treatment at 140 °C for 3 s and homogenisation at pilot-plant scale were applied to whole milk. The gastric behaviour was investigated using a recently developed semi-dynamic adult in vitro model. The emptied digesta were analysed to assess the nutrient delivery kinetics, changes in microstructure and protein digestion. All samples showed protein aggregation and coagulum formation within the first 15 min of gastric digestion at which time the pH ranged from 5.5 to 6. Homogenised samples creamed regardless of heat treatment, whereas all non-homogenised samples exhibited sedimentation. The consistency of the coagulum of the heated samples was more fragmented compared to those of the non-heated samples. Rheological analysis showed that the higher the temperature of the heat treatment, the softer the obtained coagulum and the higher the protein hydrolysis at the end of digestion. The study also confirmed that gastric emptying of caseins from milk is delayed due to coagulation in the stomach, while β-lactoglobulin was emptied throughout the gastric phase, except for UHT-treated milk. The gastric behaviour also had an impact on the lipid and protein content of the emptied chyme. The homogenised samples seemed to release more nutrients at the end of gastric digestion

INFOGEST static in vitro simulation of gastrointestinal food digestion

peer-reviewedSupplementary information is available at http://dx.doi.org/10.1038/s41596-018-0119-1 or https://www.nature.com/articles/s41596-018-0119-1#Sec45.Developing a mechanistic understanding of the impact of food structure and composition on human health has increasingly involved simulating digestion in the upper gastrointestinal tract. These simulations have used a wide range of different conditions that often have very little physiological relevance, and this impedes the meaningful comparison of results. The standardized protocol presented here is based on an international consensus developed by the COST INFOGEST network. The method is designed to be used with standard laboratory equipment and requires limited experience to encourage a wide range of researchers to adopt it. It is a static digestion method that uses constant ratios of meal to digestive fluids and a constant pH for each step of digestion. This makes the method simple to use but not suitable for simulating digestion kinetics. Using this method, food samples are subjected to sequential oral, gastric and intestinal digestion while parameters such as electrolytes, enzymes, bile, dilution, pH and time of digestion are based on available physiological data. This amended and improved digestion method (INFOGEST 2.0) avoids challenges associated with the original method, such as the inclusion of the oral phase and the use of gastric lipase. The method can be used to assess the endpoints resulting from digestion of foods by analyzing the digestion products (e.g., peptides/amino acids, fatty acids, simple sugars) and evaluating the release of micronutrients from the food matrix. The whole protocol can be completed in ~7 d, including ~5 d required for the determination of enzyme activities.COST action FA1005 INFOGEST (http://www.cost-infogest.eu/ ) is acknowledged for providing funding for travel, meetings and conferences (2011-2015). The French National Institute for Agricultural Research (INRA, www.inra.fr) is acknowledged for their continuous support of the INFOGEST network by organising and co-funding the International Conference on Food Digestion and workgroup meeting

The (193-209) 17-residues peptide of bovine b-casein is transported through Caco-2 monolayer

Although the bioavailability of large peptides with biological activity is of great interest, the intestinal transport has been described for peptides up to only nine residues. \u3b2-casein (\u3b2-CN, 193-209) is a long and hydrophobic peptide composed of 17 amino acid residues (molecular mass 1881 Da) with immunomodulatory activity. The present work examined the transport of the \u3b2-CN (193-209) peptide across Caco-2 cell monolayer. In addition, we evaluated the possible routes of the \u3b2-CN (193-209) peptide transport, using selective inhibitors of the different routes for peptide transfer through the intestinal barrier. The results showed that the \u3b2-CN (193-209) peptide resisted the action of brush-border membrane peptidases, and that it was transported through the Caco-2 cell monolayer. The main route involved in transepithelial transport of the \u3b2-CN (193-209) peptide was transcytosis via internalized vesicles, although the paracellular transport via tight-junctions could not be excluded. Our results demonstrated the transport of an intact long-chain bioactive peptide in an in vitro model of intestinal epithelium, as an important step to prove the evidence for bioavailability of this peptide

Intestinal digestion kinetics of milk proteins in humans

Milk proteins are of interest as they contain soluble (SP) and non-soluble (casein) fractions that behave differently during digestion. SP are rapidly evacuated from the stomach whereas gastric emptying of casein is delayed (Boirie et al. 1997). This difference that has been demonstrated in vitro or in vivo in animals and in humans induces differential appearance of derived peptides and amino acids in the blood and postprandial metabolic response. This study aims to assess in humans the intestinal digestion kinetics of both protein fractions. It has been performed on 16 in good health volunteers whose diets were standardized during 9 days. On the 9th day they ingested the meal composed among others of 30 g of either casein or SP. Ileal effluents were continuously collected every 30 min for 6 hours using a double lumen nasogastric tube that migrated to the jejunum. In order to verify whether casein and SP present differential digestion in jejunum, immunoreactive proteins were quantified and peptides were identified using proteomic tools (chromatography coupled on line with mass spectrometry). This study shows that i) immunoreactive proteins and peptides were present in a greater amount during the first hour of digestion for SP meal whereas a two-step digestion was observed for casein meal: a first one at 1.5-2.5 hours and a second one 4-5 hours after meal ingestion, ii) large protein fragments were present within the jejunum for both meals thus demonstrating that proteins digestion was incomplete in the jejunum, and iii) the peptides derived from casein were smaller than the ones from SP. The digestion of casein and soluble proteins differed in both the intestinal kinetics and the molecular weight of the peptides. These differences offer several applications in overweight and elderly people or in patients with wasting disorders

Intestinal digestion kinetics of casein or milk soluble proteins in humans

International audienc

Intestinal digestion kinetics of casein or milk soluble proteins in humans

International audienc

Many peptides are released in the jejunum through the digestion of casin or milk soluble proteins in humans

International audienc