Postprandial Amino Acid Research Articles

Postprandial amino acid, glucose and insulin responses among healthy adults after a single intake of Lemna minor in comparison with green peas: a randomised trial.

A high protein content combined with its enormous growth capacity make duckweed an interesting alternative protein source, but information about postprandial responses in humans is lacking. The present study aimed to assess the postprandial serum amino acid profile of Lemna minor in healthy adults in comparison with green peas. A secondary objective was to obtain insights regarding human safety. A total of twelve healthy volunteers participated in a randomised, cross-over trial. Subjects received two protein sources in randomised order with a 1-week washout period. After an overnight fast, subjects consumed L. minor or peas (equivalent to 20 g of protein). After a baseline sample, blood samples were taken 15, 30, 45, 60, 75, 90, 120, 150 and 180 min after consumption to assess amino acid, glucose and insulin levels. Heart rate, blood pressure and aural temperature were measured before and after consumption, and subjects reported on gastrointestinal discomfort for four subsequent days. Compared with green peas, significantly lower blood concentrations of amino acids from L. minor were observed, indicating lower digestibility. L. minor consumption resulted in lower plasma glucose and insulin levels compared with peas, probably due to different glucose content. There were no significant differences concerning the assessed health parameters or the number of gastrointestinal complaints, indicating that a single bolus of L. minor - grown under controlled conditions - did not induce acute adverse effects in humans. Further studies need to investigate effects of repeated L. minor intake and whether proteins purified from L. minor can be digested more easily.

The effect of casein, hydrolyzed casein, and whey proteins on urinary and postprandial plasma metabolites in overweight and moderately obese human subjects

Casein and whey proteins differ in amino acid composition and absorption rate; however, the absorption rate of casein can be increased to mimic that of whey proteins by exogenous hydrolysis. In view of these compositional differences, we studied the metabolic responses to intake of casein, hydrolyzed casein, and whey proteins in overweight and moderately obese men and women by investigating select urinary and blood plasma metabolites. A total of 21 urinary and 23 plasma metabolites were identified by nuclear magnetic resonance spectroscopy. The postprandial plasma metabolites revealed a significant diet-time interaction for isoleucine (P = 0.001) and tyrosine (P = 0.001). The level of isoleucine and tyrosine peaked 90 min postprandially with a 1.4-fold difference following intake of whey proteins compared with either casein or hydrolyzed casein. A 1.2-fold higher urinary level of lactate was observed after intake of whey proteins compared with intake of intact casein (P < 0.01). The plasma metabolites revealed different amino acid profiles reflecting the amino acid composition of casein and whey proteins. Furthermore, the results support that casein hydrolysates neither affect the postprandial amino acid absorption rate nor the amino acid level compared with that of intact casein. The urinary lactate increases following whey protein intake might indicate a higher metabolism of glucogenic amino acids. © 2018 Society of Chemical Industry.

Satiety and gastrointestinal hormones during a Mixed Meal Tolerance Test after gastric bypass surgery: association with plasma amino acid concentrations

BackgroundCirculating amino acids have been associated with both appetite and the secretion of anorexigenic hormones in healthy and obese populations. This effect has not been investigated in subjects having undergone Roux-en-Y gastric bypass surgery (RYGB). ObjectiveTo investigate the association between postprandial plasma concentrations of amino acids and the anorexigenic hormones glucagon-like peptide-1 (GLP-1) and peptide tyrosine tyrosine (PYY), the orexigenic hormone ghrelin, and satiety and hunger in post-RYGB subjects. SettingA Dutch surgical department. MethodsParticipants after primary RYGB were studied during a Mixed Meal Tolerance Test (MMTT). Satiety and hunger were assessed every 30 minutes on visual analogue scales. Blood samples were collected at baseline, every 10 minutes during the first half hour and every 30 minutes until 210 minutes after the start. The samples were assessed for 24 amino acids and 3 gastrointestinal hormones. Incremental areas under the curve (iAUCs) were calculated. Exploratory analyses were performed in which subjects were divided into high and low responders depending on the median iAUC. Results42 subjects, aged 48 ± 11 (mean ± SD) years, 31 to 76 months post-RYGB and with total weight loss of 30 ± 9% completed the MMTT. Subjects with high satiety scores had more than a 25% higher net iAUC of PYY and GLP-1 and at least a 10% higher net iAUC of 10 amino acids compared to subjects with low scores (P < 0.05). The net iAUC of five of these amino acids (i.e. arginine, asparagine, histidine, serine and threonine) was more than 10% higher in subjects with high responses on GLP-1 and/or PYY (P < 0.05). ConclusionsCertain postprandial amino acids were associated with satiety and anorexigenic hormones and could therefore play a role in appetite regulation after RYGB; either by a direct effect on satiety, indirectly through gastrointestinal hormones, or both.

Fast digestive proteins and sarcopenia of aging.

The speed of dietary protein digestion influences postprandial amino acid availability which is crucial for improving altered anabolic response of skeletal muscle one feature of sarcopenia during aging. By analogy with carbohydrate and in reference to their absorption rate, dietary proteins can be classified as 'fast' or 'slow' proteins depending on matrix food structure and technological processes, which can influence amino acids availability and their subsequent metabolic actions. 'Fast' digestive proteins have been shown to stimulate muscle protein synthesis and to improve muscle function in several recent studies involving older patients. These new aspects may be applied for improving health through preservation or restoration of muscle protein mass and function in clinical situations (obesity, rheumatoid arthritis and cancer cachexia). Using fast digestive proteins is of major interest to overcome 'anabolic resistance' of aging for limiting sarcopenia. Fast proteins' action on muscle anabolism may be stimulated by other nutrients like vitamin D or omega 3 fatty acids or by combination with exercise. The beneficial impact of the 'fast' protein concept beyond the amount of dietary protein on muscle preservation is a promising therapeutic perspective to improve mobility and quality of life of older patients affected with chronic disease.

SUN-P283: Leucine-Enriched whey Protein Medical Nutrition Drinks in Powder and Liquid Format Result in Higher Postprandial Serum Amino Acid Levels Compared to Standard Casein-Dominant Medical Nutrition Drinks

SUN-P283: Leucine-Enriched whey Protein Medical Nutrition Drinks in Powder and Liquid Format Result in Higher Postprandial Serum Amino Acid Levels Compared to Standard Casein-Dominant Medical Nutrition Drinks

Effect of light-load resistance exercise on postprandial amino acid transporter expression in elderly men.

An impaired amino acid sensing is associated with age‐related loss of skeletal muscle mass. We tested whether light‐load resistance exercise (LL‐RE) affects postprandial amino acid transporter (AAT) expression in aging skeletal muscle. Untrained, healthy men (age: +65 years) were subjected to 13 h of supine rest. After 2 1/2 h of rest, unilateral LL‐RE was conducted (leg extensions, 10 sets of 36 repetitions) at 16% 1RM. Thereafter, the subjects were randomized into groups that orally ingested 40 g of whey protein either as hourly drinks (4 g per drink) (PULSE, N = 10) or two boluses (28 g at 0 h and 12 g at 7 h) (BOLUS, N = 10), or hourly isocaloric maltodextrin drinks (placebo, N = 10). Quadriceps muscle biopsies were taken at 0, 3, 7, and 10 h postexercise from both the resting and exercised leg, from which the membrane protein and mRNA expression of select AATs were analyzed by Western Blot and RT‐PCR, respectively. LAT1 and PAT1 protein expression increased in response to LL‐RE in the PULSE group, and SNAT2 and PAT1 protein expression increased in the BOLUS group when plasma BCAA concentration was low. In all three groups, LL‐RE increased LAT1 mRNA expression, whereas a time course decrease in SNAT2 mRNA expression was observed. LL‐RE increased membrane‐associated AAT protein expression and mRNA expression. Altered AAT protein expression was only seen in groups that ingested whey protein, with the greatest effect observed after hourly feeding. This points toward an importance of AATs in the anabolic response following LL‐RE and protein intake.

Food ingestion in an upright sitting position increases postprandial amino acid availability when compared with food ingestion in a lying down position.

Dietary protein digestion and absorption kinetics determine the postprandial increase in muscle protein synthesis. We recently demonstrated that body position during feeding can modulate the postprandial rise in plasma amino acid availability. Here we investigated whether protein ingestion in an upright sitting body position accelerates gastric emptying and improves dietary protein digestion and subsequent amino acid absorption compared with feeding in a supine lying body position. In a crossover design, 8 young males (age, 26 ± 1 years; body mass index, 24.0 ± 0.9 kg·m-2) ingested 20 g intrinsically l-[1-13C]-phenylalanine-labeled milk protein plus 1.5 g paracetamol while sitting in an upright position or lying down in a supine position. Blood samples were collected frequently during a 5-h postprandial period. Gastric emptying rates and dietary protein digestion and absorption were assessed using plasma paracetamol and amino acid concentrations as well as plasma l-[1-13C]-phenylalanine enrichments. Peak plasma leucine concentrations were higher when protein was ingested in an upright sitting versus lying position (213 ± 15 vs 193 ± 12 μmol·L-1, P < 0.05), which was accompanied by a trend for a greater overall leucine response (13 989 ± 720 vs 11 875 ± 1073 AU, respectively; P = 0.05). Peak plasma paracetamol concentrations were higher in the sitting versus lying treatment (11.6 ± 0.5 vs 9.3 ± 0.6 mg·L-1, P < 0.05). Protein ingestion in an upright sitting position accelerates gastric emptying and increases the postprandial rise in plasma amino acid availability by increasing protein digestion and amino acid absorption rates. Therefore, feeding in an upright body position as opposed to a lying position is an important prerequisite to allow proper postprandial muscle protein accretion.

Satiety and memory enhancing effects of a high-protein meal depend on the source of protein

Objective: High- protein diets have become increasingly popular with various touted benefits. However, the extent to which protein quantity and source affects cognitive functioning through altering postprandial amino acid profiles has not been investigated. Further, whether all protein sources are similarly anorexigenic is uncertain. The objective of this study was to determine the influence of protein level and source on Barnes maze performance, satiety and plasma amino acid levels in male Sprague-Dawley rats.Methods: Rats were entrained to a meal-feeding schedule consisting of a 30 minutes meal, equivalent to 20% of average daily intake, one hour into the dark phase then ad libitum access to food for 5 h. On test days, rats received one of three isocaloric diets as their first meal, hereafter referred to as Egg White (EW), Wheat Gluten (WG), or Basal, and then were measured for cognitive performance, feeding behavior, or plasma amino acid levels via jugular catheter. Percentage energy from protein was 35% for both EW and WG and 20% for Basal with equal amounts provided by EW and WG proteins.Results: Rats provided EW performed similarly to Basal on the Barnes maze, whereas WG performed worse. EW increased satiety, whereas WG reduced satiety relative to Basal. Both EW and WG increased postprandial concentrations of large neutral and branched chain amino acids relative to Basal, but in EW, concentrations were slower to peak, and peaked to a higher level than WG.Discussion: Results demonstrate the importance of protein source for cognition and satiety enhancing effects of a high-protein meal.

The impact of liquid preloads varying in macronutrient content on postprandial kinetics of amino acids relative to appetite in healthy adults

The underlying mechanisms for the effect of proteins on appetite regulation, especially in presence of variable macronutrient composition, are not fully elucidated. The present study investigated the absorption kinetics of proteins after co-ingestion with the other macronutrients and examined the impact of circulating amino acids on appetite and satiety-related gut hormones. A randomized, within-subjects, 2-level full factorial design was implemented, where thirty six healthy subjects consumed seven preloads with similar energy density (3.1 kJ/g) and volume (670 mL) but with varying macronutrient content. The energy from protein (%) and the CHO:fat ratio were the two factors combined in three levels of 9, 24, 40 and 0.4, 2, 3.6 respectively. Blood and appetite parameters were evaluated until the serving of the ad libitum lunch after 210 min and the amino acid concentrations were measured in a subgroup of seven male subjects. The amino acid concentrations peaked at 90 min after all preloads and returned to the baseline values until 210 min. Protein intake affected amino acid profiles (P < 0.05), while no differences (P > 0.05) were detected between the two high protein preloads despite the different CHO:fat ratio (40%/0.4 CHO:fat and 40%/3.6 CHO:fat), indicating that neither carbohydrate nor fat influenced the profiles. Most of the amino acids were not related to appetite sensations or gut hormones (P > 0.05), while glutamate was positively associated with prospective consumption and inversely related to ghrelin (P < 0.05). Valine, leucine, isoleucine, lysine and α-aminobutyric acid were inversely associated with energy intake (P < 0.05). Overall, postprandial amino acid profiles were solely affected by protein content and were not consistently related to appetite regulation. Further investigation of glutamate's effect on appetite is needed.

Amino Acid and Biogenic Amine Profile Deviations in an Oral Glucose Tolerance Test: A Comparison between Healthy and Hyperlipidaemia Individuals Based on Targeted Metabolomics.

Hyperlipidemia (HLP) is characterized by a disturbance in lipid metabolism and is a primary risk factor for the development of insulin resistance (IR) and a well-established risk factor for cardiovascular disease and atherosclerosis. The aim of this work was to investigate the changes in postprandial amino acid and biogenic amine profiles provoked by an oral glucose tolerance test (OGTT) in HLP patients using targeted metabolomics. We used ultra-high-performance liquid chromatography-triple quadrupole mass spectrometry to analyze the serum amino acid and biogenic amine profiles of 35 control and 35 HLP subjects during an OGTT. The amino acid and biogenic amine profiles from 30 HLP subjects were detected as independent samples to validate the changes in the metabolites. There were differences in the amino acid and biogenic amine profiles between the HLP individuals and the healthy controls at baseline and after the OGTT. The per cent changes of 13 metabolites from fasting to the 2 h samples during the OGTT in the HLP patients were significantly different from those of the healthy controls. The lipid parameters were associated with the changes in valine, isoleucine, creatine, creatinine, dimethylglycine, asparagine, serine, and tyrosine (all p < 0.05) during the OGTT in the HLP group. The postprandial changes in isoleucine and γ-aminobutyric acid (GABA) during the OGTT were positively associated with the homeostasis model assessment of insulin resistance (HOMA-IR; all p < 0.05) in the HLP group. Elevated oxidative stress and disordered energy metabolism during OGTTs are important characteristics of metabolic perturbations in HLP. Our findings offer new insights into the complex physiological regulation of metabolism during the OGTT in HLP.

Body Position Modulates Gastric Emptying and Affects the Post-Prandial Rise in Plasma Amino Acid Concentrations Following Protein Ingestion in Humans.

Dietary protein digestion and amino acid absorption kinetics determine the post-prandial muscle protein synthetic response. Body position may affect gastrointestinal function and modulate the post-prandial rise in plasma amino acid availability. We aimed to assess the impact of body position on gastric emptying rate and the post-prandial rise in plasma amino acid concentrations following ingestion of a single, meal-like amount of protein. In a randomized, cross-over design, eight healthy males (25 ± 2 years, 23.9 ± 0.8 kg·m−2) ingested 22 g protein and 1.5 g paracetamol (acetaminophen) in an upright seated position (control) and in a −20° head-down tilted position (inversion). Blood samples were collected during a 240-min post-prandial period and analyzed for paracetamol and plasma amino acid concentrations to assess gastric emptying rate and post-prandial amino acid availability, respectively. Peak plasma leucine concentrations were lower in the inversion compared with the control treatment (177 ± 15 vs. 236 ± 15 mmol·L−1, p < 0.05), which was accompanied by a lower plasma essential amino acid (EAA) response over 240 min (31,956 ± 6441 vs. 50,351 ± 4015 AU; p < 0.05). Peak plasma paracetamol concentrations were lower in the inversion vs. control treatment (5.8 ± 1.1 vs. 10.0 ± 0.6 mg·L−1, p < 0.05). Gastric emptying rate and post-prandial plasma amino acid availability are significantly decreased after protein ingestion in a head-down tilted position. Therefore, upright body positioning should be considered when aiming to augment post-prandial muscle protein accretion in both health and disease.

Postprandial metabolomics: A pilot mass spectrometry and NMR study of the human plasma metabolome in response to a challenge meal

The study of postprandial metabolism is relevant for understanding metabolic diseases and characterizing personal responses to diet. We combined three analytical platforms – gas chromatography-mass spectrometry (GC-MS), liquid chromatography-mass spectrometry (LC-MS) and nuclear magnetic resonance (NMR) – to validate a multi-platform approach for characterizing individual variation in the postprandial state. We analyzed the postprandial plasma metabolome by introducing, at three occasions, meal challenges on a usual diet, and 1.5 years later, on a modified background diet. The postprandial response was stable over time and largely independent of the background diet as revealed by all three analytical platforms. Coverage of the metabolome between NMR and GC-MS included more polar metabolites detectable only by NMR and more hydrophobic compounds detected by GC-MS. The variability across three separate testing occasions among the identified metabolites was in the range of 1.1–86% for GC-MS and 0.9–42% for NMR in the fasting state at baseline. For the LC-MS analysis, the coefficients of variation of the detected compounds in the fasting state at baseline were in the range of 2–97% for the positive and 4–69% for the negative mode. Multivariate analysis (MVA) of metabolites detected with GC-MS revealed that for both background diets, levels of postprandial amino acids and sugars increased whereas those of fatty acids decreased at 0.5 h after the meal was consumed, reflecting the expected response to the challenge meal. MVA of NMR data revealed increasing postprandial levels of amino acids and other organic acids together with decreasing levels of acetoacetate and 3-hydroxybutanoic acid, also independent of the background diet. Together these data show that the postprandial response to the same challenge meal was stable even though it was tested 1.5 years apart, and that it was largely independent of background diet. This work demonstrates the efficacy of a multi-platform metabolomics approach followed by multivariate and univariate data analysis for a broad-scale screen of the individual metabolome, particularly for studies using repeated measures to determine dietary response phenotype.

Differences in postprandial protein handling after beef compared with milk ingestion during postexercise recovery: a randomized controlled trial

Protein consumed after resistance exercise increases postexercise muscle protein synthesis rates. To date, dairy protein has been studied extensively, with little known about the capacity of other protein-dense foods to augment postexercise muscle protein synthesis rates. We aimed to compare protein digestion and absorption kinetics, postprandial amino acid availability, anabolic signaling, and the subsequent myofibrillar protein synthetic response after the ingestion of milk compared with beef during recovery from resistance-type exercise. In crossover trials, 12 healthy young men performed a single bout of resistance exercise. Immediately after cessation of exercise, participants ingested 30 g protein by consuming isonitrogenous amounts of intrinsically l-[1-(13)C]phenylalanine-labeled beef or milk. Blood and muscle biopsy samples were collected at rest and after exercise during primed continuous infusions of l-[ring-(2)H5]phenylalanine and l-[ring-3,5-(2)H2]tyrosine to assess protein digestion and absorption kinetics, plasma amino acid availability, anabolic signaling, and subsequent myofibrillar protein synthesis rates in vivo in young men. Beef protein-derived phenylalanine appeared more rapidly in circulation compared with milk ingestion (P < 0.001). The availability of phenylalanine during the 5-h postexercise period tended to be higher after beef (64% ± 3%) ingestion than after milk ingestion (57% ± 3%; P = 0.08). Both beef and milk ingestion were followed by an increase in the phosphorylation of mammalian target of rapamycin complex 1 and 70-kDa S6 protein kinase 1 during postexercise recovery. Milk ingestion increased myofibrillar protein synthesis rates to a greater extent than did beef ingestion during the 0- to 2-h postexercise phase (P = 0.013). However, the increase in myofibrillar protein synthesis rates did not differ between milk and beef ingestion during the entire 0- to 5-h postexercise phase (P = 0.114). Both milk and beef ingestion augment the postexercise myofibrillar protein synthetic response in young men, with a stronger stimulation of myofibrillar protein synthesis during the early postprandial stage after milk ingestion. This trial was registered at www.clinicaltrials.gov as NCT01578590.

Postprandial Differences in the Amino Acid and Biogenic Amines Profiles of Impaired Fasting Glucose Individuals after Intake of Highland Barley.

The aim of this study was to measure the postprandial changes in amino acid and biogenic amine profiles in individuals with impaired fasting glucose (IFG) and to investigate the changes of postprandial amino acid and biogenic amine profiles after a meal of highland barley (HB). Firstly, 50 IFG and 50 healthy individuals were recruited for the measurement of 2 h postprandial changes of amino acid and biogenic amine profiles after a glucose load. Secondly, IFG individuals received three different loads: Glucose (GL), white rice (WR) and HB. Amino acid and biogenic amine profiles, glucose and insulin were assayed at time zero and 30, 60, 90 and 120 min after the test load. The results showed fasting and postprandial amino acid and biogenic amine profiles were different between the IFG group and the controls. The level of most amino acids and their metabolites decreased after an oral glucose tolerance test, while the postprandial level of γ-aminobutyric acid (GABA) increased significantly in IFG individuals. After three different test loads, the area under the curve for glucose, insulin, lysine and GABA after a HB load decreased significantly compared to GL and WR loads. Furthermore, the postprandial changes in the level of GABA between time zero and 120 min during a HB load were associated positively with 2 h glucose and fasting insulin secretion in the IFG individuals. Thus, the HB load produced low postprandial glucose and insulin responses, which induced changes in amino acid and biogenic amine profiles and improved insulin sensitivity.

Protein type and caloric density of protein supplements modulate postprandial amino acid profile through changes in gastrointestinal behaviour: A randomized trial

The requirement of leucine and essential amino acids (EAA) to stimulate muscle protein synthesis increases with age. To target muscle anabolism it is suggested that higher postprandial blood levels of leucine and EAA are needed in older people. The aim was to evaluate the impact of oral nutritional supplements with distinct protein source and energy density, resembling mixed meals, on serum amino acid profiles and on gastrointestinal behaviour. Four iso-nitrogenous protein (21 g) supplements were studied containing leucine-enriched whey protein with 150/320 kcal (W150/W320) or casein protein with 150/320 kcal (C150/C320); all products contained carbohydrates (10 or 32 g) and fat (3 or 12 g). Postprandial serum AA profiles were evaluated in twelve healthy, older subjects who participated in a randomized, controlled, single blind, cross-over study. Gastrointestinal behaviour was studied in vitro by looking at gastric coagulation and cumulative intestinal protein digestion over time. The peak serum leucine concentration was twofold higher for W150 vs. C150 (521 ± 15 vs. 260 ± 15 μmol/L, p < 0.001), higher for W320 vs. C320 (406 ± 15 vs. 228 ± 15 μmol/L, p < 0.001), and higher for low-caloric vs. high-caloric products (p < 0.001 for pooled analyses; p < 0.001 for interaction protein source*caloric density). Similar effects were observed for the peak concentrations of EAA and total AA (TAA). In vitro gastric coagulation was observed only for the casein protein supplements. Intestinal digestion for 90 min resulted in higher levels of free TAA, EAA, and leucine for W150 vs. C150, for W150 vs. W320, and for C150 vs. C320 (p < 0.0125). A low caloric leucine-enriched whey protein nutritional supplement provides a higher rise in serum levels of TAA, EAA and leucine compared to casein protein or high caloric products in healthy, elderly subjects. These differences appear to be mediated in part by the gastrointestinal behaviour of these products. ClinicalTrials.gov: NCT02013466.

Post-prandial amino acid and leucine responses to serum albumin concentrate compared to whey protein concentrate in healthy subjects

Background Supplemental protein sources vary in composition in regards to size, structure, and amino acid composition of the varying individual proteins. Serum albumin concentrate (SA) is a new protein source extracted from edible-grade bovine plasma, which was recently made available on commercial scale. As compared to the low MW proteins in whey protein concentrate (WPC), SA consists of higher MW protein constituents such as albumin (66kD, >60%) and globulin proteins (130 kD, >10%), which contain a high quality amino acid composition. These differences in the protein profile of SA may both delay and sustain amino acid absorption in comparison to WPC. The objective of this study was to determine the post-prandial amino acid response to oral ingestion of SA and to compare the response to that of WPC. Methods Eight healthy, 20-30 year old, male (n=4, 80.3 kg BW) and female (n=4, 63.7 kg BW) volunteers participated in an open label, clinical study utilizing a cross-over design (Clinicaltrials.gov: NCT01643265). The volunteers received each of the two protein sources in a random order with a 7 d washout period between treatments. After a 12 h overnight fast, 7 mL of blood was collected from a catheter inserted into a forearm vein. Baseline amino acid values at 30 and 15 min were determined prior to administration of the experimental protein sources. Twenty grams of either WPC or SA was provided in 335 mL of water. Subsequent blood samples were collected at 15, 30, 45, 60, 90, 120, 180, and 210 min after ingestion for analysis of individual amino acid concentrations. An EZ:faastTM amino acid analysis kit was used for sample pretreatment and chromatographic separation was conducted using a Agilent 6460 triple quadrupole LC/MS system. Data were analyzed using repeated measures and General Linear Models procedures from SAS (Version 9.2) including treatment, gender, and test period as independent variables in the statistical model. Significance is reported as P<0.05 and P<0.01. Consent to publish the results was obtained from all participants. Results Total plasma amino acid concentration at baseline was found to be higher (P<0.01) at baseline in male subjects (2,633 nmoles/mL) compared to female subjects (2,153 nmoles/mL). In contrast, plasma leucine concentration was found to be higher (P<0.05) in female subjects (156 nmoles/mL) compared to male subjects (103 nmoles/mL). Rises in post-prandial individual amino acid concentration were observed for both WPC and SA (P<0.01). The rises reflect the amino acid pattern of the protein source ingested. The ingestion of whey protein concentrate increased plasma total amino acid concentration 30 min post-prandially compared to SA (P<0.05) by 10%, without differences in leucine. In contrast, the ingestion of SA promoted 14% higher leucine concentrations 120 min post-prandially than did WPC (P<0.05). Conclusion Individual post-prandial amino acids reflect the amino acid pattern and characteristics of the protein source ingested. The digestion and absorption of the protein and amino acid composition of serum albumin concentrate

OP026: Intensive Exercise Hampers the Postprandial Citrulline Bioavailability Following Casein Bolus Feeding

Rationale: Metabolic stress like surgery and intensive exercise have been reported to increase intestinal permeability. It is not known whether intensive exercise also influences gut metabolic functioning. The effects of intensive exercise on intestinal permeability, postprandial amino acid (AA) bioavailability and intestinal enterocyte metabolic mass were determined in the human intervention study Protege.

Evidence of Enhanced Serum Amino Acid Profile but Not Appetite Suppression by Dietary Glycomacropeptide (GMP): A Comparison of Dairy Whey Proteins

Objective: There is evidence that high-protein foods increase satiety and may aid weight loss, yet little is known of differential effects of protein composition. The aim of the study was to compare the acute effects of 4 whey proteins on satiety and food intake and to evaluate possible relationships with postprandial serum amino acid concentrations. Methods: Isoenergetic high-protein shakes (∼1 MJ) containing 25 g whey protein were given to 18 lean male participants using a crossover design. Three protein fractions identified as satiating in a rat model, glycomacropeptide (GMP), beta-lactoglobulin (ß-lac), and colostrum whey protein concentrate (WPC), were compared with a WPC control. A standardized 2.5MJ breakfast was given at 0830 hours, followed by the preload beverages at 1130 hours. Participants rated appetite sensations using visual analogue scales (VAS) prior to the beverage (baseline, 0 minutes) and then at 15, 30, 45, 60, 90, 150, and 210 minutes. Energy and macronutrient intake was measured by covert weighing of an ad libitum lunch meal at 90 minutes. Repeat blood samples were collected via venous cannulation. Results: Serum amino acid (a.a.) concentrations differed between whey fractions (p = 0.012) and were higher following GMP compared to ß-lac (p = 0.051) and colostrum WPC (p = 0.044) but not the WPC control (p = 0.20). There was no difference in VAS-rated hunger, satisfaction, or thoughts of food between whey fractions, but fullness did differ (p = 0.032) and was highest following the ß-lac beverage. Energy intake was not suppressed relative to control by any of the 3 whey fractions. Conclusions: We conclude that total serum a.a. concentration was a poor indicator of satiety, with little evidence of differential satiety between these whey proteins other than a modest enhancement of fullness by ß-lac.

Nutritional evaluation of rapeseed protein compared to soy protein for quality, plasma amino acids, and nitrogen balance – A randomized cross-over intervention study in humans

Plant proteins such as rapeseed have received little attention for human nutrition due to their high level of antinutritive compounds. Today, newer technologies can eliminate such compounds. The present intervention study aimed to evaluate nutritional and physiological properties of two manufactured canola proteins with special focus on their bioavailability in humans. 28 healthy male subjects (ø 25 years) consumed 30.0 g protein (canola protein isolate--CPI, canola protein hydrolyzate--CPH or soy protein isolate--SPI) in a randomized, double-blind, cross-over study. Blood samples were regularly drawn over the 8-h postprandial period and a 24-h urine sample was collected. True digestibility of the canola proteins determined in a separate rat assay showed 93.3% for CPI and 97.3% for CPH. In humans, consumption of either 30.0 g canola protein or soy protein mixed in a drink led to significant increases in plasma amino acids after 62.3 and 83.6 min, respectively. While the CPH produced an earlier response compared to CPI and SPI, total amino acid response (AUC for 8 h) was comparable between all interventions. The nitrogen balance between the three proteins tested showed no statistical differences. High digestibility of rapeseed protein was found in rats. In humans, this is the first intervention study showing rapeseed protein (both isolate and hydrolyzate) as having a high nutritional quality and can be considered to be as efficient as soy protein for a postprandial amino acid response. This trial was registered at ClinicalTrials.gov Identifier: NCT01481584.

Artemia protein is processed very fast in Solea senegalensis larvae: A dynamic simulation model

Further improvement of growth performance in fish larviculture is closely linked to better understanding of the dietary amino acid (AA) requirements, and therefore of the processes involved in AA metabolism. In recent years, major advances in the understanding of fish larvae amino acid metabolism have been accomplished, in particular through the use of tracer studies. Modelling is a holistic approach to integrate knowledge on growth and metabolism and identify gaps in current understanding. A dynamic mechanistic model that simulates AA metabolism of fish larvae was developed. It aims to improve the understanding of larval digestion and absorption of dietary AA, and the postprandial AA metabolism and growth. The model also assists in the interpretation of results obtained from tracer studies. The model is driven by amino acid intake, with the absorbed dietary AA being used for energy production or for biosynthetic processes. The model is implemented for Senegalese sole (Solea senegalensis) larvae fed Artemia, and was parameterized using literature data. The model allows to integrate the results obtained after feeding a single meal with tracer AA, and following these tracer AA in the free AA and protein pools of larval gut and larval body at different time points after the meal. Model simulations suggest that there is a sharp dynamic change in the FAA pool after a meal while the protein pool is little affected. This suggests that the AA composition of the food has a major contribution to the FAA pool composition. This implies that sole larvae is highly sensitive to dietary AA imbalances, having high AA unavoidable losses unless the dietary AA profile is well balanced. The model also suggests that rates of protein synthesis and AA catabolism rapidly increases after the meal, with the peak for this postprandial metabolism occurring only 1h after the meal, and the rates returning to “basal” values 2h after the meal. This suggests a rapid processing of the Artemia protein by the larvae, and supports the need for feeding sole larvae at a high frequency in order to fully use its growth potential. Mechanistic modelling is useful and an important complement in evaluation of metabolism kinetics in nutrient flux studies. Moreover, due to its mechanistic nature, the present model can be used with different AA tracers, and also for other fish species.