Ingestion of a protein hydrolysate, as opposed to its intact protein, accelerates protein digestion and absorption from the gut, augments postprandial amino acid availability, and tends to increase the incorporation rate of dietary amino acids into skeletal muscle protein.

Protein ingestion before sleep represents an effective dietary strategy to augment muscle mass and strength gains during resistance exercise training in young men. This trial was registered at clinicaltrials.gov as NCT02222415.

Impaired digestion and/or absorption of dietary protein lowers postprandial plasma amino acid availability and, as such, could reduce the postprandial muscle protein synthetic response in the elderly. We aimed to compare in vivo dietary protein digestion and absorption and the subsequent postprandial muscle protein synthetic response between young and elderly men. Ten elderly (64 +/- 1 y) and 10 young (23 +/- 1 y) healthy males consumed a single bolus of 35 g specifically produced, intrinsically l-[1-(13)C]phenylalanine-labeled micellar casein (CAS) protein. Furthermore, primed continuous infusions with l-[ring-(2)H(5)]phenylalanine, l-[1-(13)C]leucine, and l-[ring-(2)H(2)]tyrosine were applied and blood and muscle tissue samples were collected to assess the appearance rate of dietary protein-derived phenylalanine in the circulation and the subsequent muscle protein fractional synthetic rate over a 6-h postprandial period. Protein ingestion resulted in a rapid increase in exogenous phenylalanine appearance in both the young and elderly men. Total exogenous phenylalanine appearance rates (expressed as area under the curve) were 39 +/- 3 mumol.6 h.kg(-1) in the young men and 38 +/- 2 mumol.6 h.kg(-1) in the elderly men (P = 0.73). In accordance, splanchnic amino acid extraction did not differ between young (72 +/- 2%) and elderly (73 +/- 1%) volunteers (P = 0.74). Muscle protein synthesis rates, calculated from the oral tracer, were 0.063 +/- 0.006 and 0.054 +/- 0.004%/h in the young and elderly men, respectively, and did not differ between groups (P = 0.27). We conclude that protein digestion and absorption kinetics and the subsequent muscle protein synthetic response following the ingestion of a large bolus of intact CAS are not substantially impaired in healthy, elderly men.

The present study was designed to assess the impact of coingestion of various amounts of carbohydrate combined with an ample amount of protein intake on postexercise muscle protein synthesis rates. Ten healthy, fit men (20 Ϯ 0.3 yr) were randomly assigned to three crossover experiments. After 60 min of resistance exercise, subjects consumed 0.3 g ⅐ kg Ϫ1 ⅐ h Ϫ1 protein hydrolysate with 0, 0.15, or 0.6 g ⅐ kg Ϫ1 ⅐ h Ϫ1 carbohydrate during a 6-h recovery period (PRO, PRO ϩ LCHO, and PRO ϩ HCHO, respectively). Primed, continuous infusions with L-[ring-13 C6]phenylalanine, L-[ring-2 H2]tyrosine, and [6,6-2 H2]glucose were applied, and blood and muscle samples were collected to assess whole body protein turnover and glucose kinetics as well as protein fractional synthesis rate (FSR) in the vastus lateralis muscle over 6 h of postexercise recovery. Plasma insulin responses were significantly greater in PRO ϩ HCHO compared with PRO ϩ LCHO and PRO (18.4 Ϯ 2.9 vs. 3.7 Ϯ 0.5 and 1.5 Ϯ 0.2 U ⅐ 6 h Ϫ1 ⅐ l Ϫ1 , respectively, P Ͻ 0.001). Plasma glucose rate of appearance (Ra) and disappearance (Rd) increased over time in PRO ϩ HCHO and PRO ϩ LCHO, but not in PRO. Plasma glucose Ra and R d were substantially greater in PRO ϩ HCHO vs. both PRO and PRO ϩ LCHO (P Ͻ 0.01). Whole body protein breakdown, synthesis, and oxidation rates, as well as whole body protein balance, did not differ between experiments. Mixed muscle protein FSR did not differ between treatments and averaged 0.10 Ϯ 0.01, 0.10 Ϯ 0.01, and 0.11 Ϯ 0.01%/h in the PRO, PRO ϩ LCHO, and PRO ϩ HCHO experiments, respectively. In conclusion, coingestion of carbohydrate during recovery does not further stimulate postexercise muscle protein synthesis when ample protein is ingested. resistance exercise; protein metabolism; nutrition; recovery POSTEXERCISE NUTRITION IS INSTRUMENTAL to enhance recovery and to facilitate the adaptive response to regular exercise training (28). In the endurance-trained athlete, rapid restoration of depleted muscle glycogen stores is essential to enhance postexercise recovery and, as such, to maintain performance capacity (15). Therefore, endurance athletes generally aim to maximize postexercise muscle glycogen synthesis rates by ingesting large amounts of carbohydrate during recovery (30,40). Coingestion of relative small amounts of protein and/or amino acids has been suggested to further accelerate muscle glycogen repletion and/or to reduce muscle damage (40, 44).It has been firmly established (4,18,19,23,25) that postexercise protein and/or amino acid intake is essential to allow net muscle protein accretion. Therefore, athletes involved in resistance-type exercise training like fitness and bodybuilding generally ingest large quantities of protein during postexercise recovery to augment net muscle protein accretion (21, 38). It is generally assumed that carbohydrate should be coingested to maximize the postexercise muscle protein synthetic response. Although ingestion of only carbohydrate does not seem to stimulate postexercise muscle protein...

An experiment was conducted to examine the effects of adding microbial phytase (Natuphos) on the performance in broilers fed a phosphorus-adequate, lysine-deficient diet. A wheat-soybean meal-sorghum-based diet, containing 1.00% lysine and 0.45% nonphytate phosphorus, was supplemented with L-lysine monochloride to provide 1.06, 1.12, or 1.18% lysine or with 125, 250, 375, 500, 750, or 1,000 phytase units (FTU)/kg diet. Each diet was fed to six pens of 10 chicks each from Day 7 to 28 posthatching. Addition of lysine to the lysine-deficient diet linearly increased (P < 0.001) weight gain and gain per feed of broilers. The response in weight gain to added phytase reached a plateau at 500 FTU/kg diet (quadratic effect, P < 0.001). Phytase had no effect on gain per feed to 250 FTU/kg diet and then increased (quadratic effect, P < 0.05) with further additions. Assuming that the observed responses in weight gain and gain per feed to added phytase were due to the release of lysine alone and by solving linear or nonlinear response equations of lysine and phytase levels, the lysine equivalency value was calculated to be 500 FTU phytase/kg diet = 0.074% lysine. Addition of increasing levels of supplemental phytase to the lysine-deficient diet improved (P < 0.001) the digestibilities of nitrogen and all amino acids. Phytase also increased the AME, and the response reached a plateau at 750 FTU/kg diet (quadratic effect, P < 0.001). These results showed that amino acid and energy responses are responsible for the performance improvements observed when phytase was added to a wheat-soybean meal-sorghum-based diet.

The amount of dietary protein is associated with intestinal disease in different vertebrate species. In humans, this is exemplified by the association between high-protein intake and fermentation metabolite concentrations in patients with inflammatory bowel disease. In production animals, dietary protein intake is associated with postweaning diarrhea in piglets and with the occurrence of wet litter in poultry. The underlying mechanisms by which dietary protein contributes to intestinal problems remain largely unknown. Fermentation of undigested protein in the hindgut results in formation of fermentation products including short-chain fatty acids, branched-chain fatty acids, ammonia, phenolic and indolic compounds, biogenic amines, hydrogen sulfide, and nitric oxide. Here, we review the mechanisms by which these metabolites may cause intestinal disease. Studies addressing how different metabolites induce epithelial damage rely mainly on cell culture studies and occasionally on mice or rat models. Often, contrasting results were reported. The direct relevance of such studies for human, pig, and poultry gut health is therefore questionable and does not suffice for the development of interventions to improve gut health. We discuss a roadmap to improve our understanding of gut metabolites and microbial species associated with intestinal health in humans and production animals and to determine whether these metabolite/bacterial networks cause epithelial damage. The outcomes of these studies will dictate proof-of-principle studies to eliminate specific metabolites and or bacterial strains and will provide the basis for interventions aiming to improve gut health.

Oral or intravenous administration of labeled, free amino acids does not allow the direct assessment of protein digestion and absorption kinetics following dietary protein intake. Consequently, dietary protein sources with labeled amino acids incorporated within the protein are required. The aim of this study was to produce milk proteins intrinsically labeled with l-[1-(13)C]phenylalanine that would allow the assessment of protein digestion and absorption kinetics and the subsequent muscle protein synthetic response to dietary protein intake in vivo in humans. Two Holstein cows (body weight of 726 +/- 38 kg) were continuously infused with l-[1-(13)C]phenylalanine at 402 micromol/min for 44 to 48 h, during and after which plasma samples and milk were collected. After milk protein separation, casein was used in a subsequent human proof-of-principle experiment. Two healthy males (aged 61 +/- 1 yr; body mass index of 22.4 +/- 0.1 kg/m(2)) ingested 35 g of casein highly enriched with [1-(13)C] phenylalanine. Plasma samples were collected at regular intervals, and skeletal muscle biopsies were collected before and 6 h after casein ingestion. In the initial experiment, a total of 5.83 kg of l-[1-(13)C]phenylalanine-enriched milk protein (casein enrichment was 29.4 molar percent excess) was collected during stable isotope infusion in the cows. In the proof-of-principle study, ingestion of 35 g of intrinsically labeled casein resulted in peak plasma l-[1-(13)C]phenylalanine enrichments within 90 min after protein ingestion (9.75 +/- 1.47 molar percent excess). Skeletal muscle protein synthesis rates calculated over the entire 6-h period averaged 0.058 +/- 0.012%/h. The production of intrinsically labeled milk protein is feasible and provides dietary protein that can be used to investigate protein digestion and absorption and the subsequent muscle protein synthetic response in vivo in humans.

The interaction between protein and phytate was investigated in vitro using proteins extracted from five common feedstuffs and from casein. The appearance of naturally present soluble protein-phytate complexes in the feedstuffs, the formation of complexes at different pHs, and the degradation of these complexes by pepsin and/or phytase were studied. Complexes of soluble proteins and phytate in the extracts appeared in small amounts only, with the possible exception of rice pollards. Most proteins dissolved almost completely at pH 2, but not after addition of phytate. Phytase prevented precipitation of protein with phytate. Pepsin could release protein from a precipitate, but the rate of release was increased by phytase. Protein was released faster from a protein-phytate complex when phytase was added, but phytase did not hydrolyze protein. Protein was released from the complex and degraded when both pepsin and phytase were added. It appears that protein-phytate complexes are mainly formed at low pH, as occurs in the stomach of animals. Phytase prevented the formation of the complexes and aided in dissolving them at a faster rate. This might positively affect protein digestibility in animals.