Plasma Amino Acid Responses Research Articles

Amino acid transport dynamics in the jejunum and ileum in rats: a regional and time-course analysis.

Postprandially, amino acids and di/tripeptides are thought to be primarily absorbed in the proximal small intestine. However, there have been no in vivo demonstrations of regional differences in amino acid transport dynamics between the proximal and distal small intestines. We monitored plasma amino acid responses in the jejunal and ileal mesenteric veins of rats after oral administration of a diet or an amino acid mixture (Expt 1) and in the portal vein after direct administration of the amino acid mixture into the lumen of the jejunum or ileum (Expt 2). In Expt 1, the total and some amino acid concentrations in the jejunal mesenteric vein were slightly higher than those in the ileal mesenteric vein after oral administration of the amino acid mixture, suggesting that the ileum actively transports luminal amino acids to the basolateral side, comparable to the jejunum. In Expt 2, portal amino acid concentrations were elevated to a greater extent after direct administration of the amino acid mixture into the ileal lumen than into the jejunal lumen. These results demonstrate regional differences in amino acid transport dynamics in vivo and suggest that the ileum has a higher capacity for transporting amino acids than the jejunum. Our findings highlight the importance of the ileum in postprandial amino acid absorption and metabolism.

Postprandial plasma amino acid and appetite responses with ingestion of a novel salmon-derived protein peptide in healthy young adults.

This study assessed postprandial plasma aminoacidemia, glycemia, insulinemia and appetite responses to ingestion of a novel salmon-derived protein peptide (Salmon PP) compared with milk protein isolate (Milk PI). In a randomised, participant-blind crossover design, eleven healthy adults (M = 5, F = 6; mean ± sd age: 22 ± 3 years; BMI: 24 ± 3 kg/m2) ingested 0·3 g/kg/body mass of Salmon PP or Milk PI. Arterialised blood samples were collected whilst fasted and over a 240-min postprandial period. Appetite sensations were measured via visual analogue scales. An ad libitum buffet-style test meal was administered after each trial. The incremental AUC (iAUC) plasma essential amino acid (EAA) response was similar between Salmon PP and Milk PI. The iAUC plasma leucine response was significantly greater following Milk PI ingestion (P < 0·001), whereas temporal and iAUC plasma total amino acid (P = 0·001), non-essential amino acid (P = 0·002), glycine (P = 0·0025) and hydroxyproline (P < 0·001) responses were greater following Salmon PP ingestion. Plasma insulin increased similarly above post-absorptive values following Salmon PP and Milk PI ingestion, whilst plasma glucose was largely unaltered. Indices of appetite were similarly altered following Salmon PP and Milk PI ingestion, and total energy and macronutrient intake during the ad libitum meal was similar between Salmon PP and Milk PI. The postprandial plasma EAA, glycine, proline and hydroxyproline response to Salmon PP ingestion suggest this novel protein source could support muscle and possibly connective tissue adaptive remodelling, which warrants further investigation, particularly as the plasma leucine response to Salmon PP ingestion was inferior to Milk PI.

Ingestion of a variety of non-animal-derived dietary protein sources results in diverse postprandial plasma amino acid responses which differ between young and older adults.

Whole-body tissue protein turnover is regulated, in part, by the postprandial rise in plasma amino acid concentrations, although minimal data exist on the amino acid response following non-animal-derived protein consumption. We hypothesised that the ingestion of novel plant- and algae-derived dietary protein sources would elicit divergent plasma amino acid responses when compared with vegan- and animal-derived control proteins. Twelve healthy young (male (m)/female (f): 6/6; age: 22 ± 1 years) and 10 healthy older (m/f: 5/5; age: 69 ± 2 years) adults participated in a randomised, double-blind, cross-over trial. During each visit, volunteers consumed 30 g of protein from milk, mycoprotein, pea, lupin, spirulina or chlorella. Repeated arterialised venous blood samples were collected at baseline and over a 5-h postprandial period to assess circulating amino acid, glucose and insulin concentrations. Protein ingestion increased plasma total and essential amino acid concentrations (P < 0·001), to differing degrees between sources (P < 0·001), and the increase was further modulated by age (P < 0·001). Postprandial maximal plasma total and essential amino acid concentrations were highest for pea (2828 ± 106 and 1480 ± 51 µmol·l-1) and spirulina (2809 ± 99 and 1455 ± 49 µmol·l-1) and lowest for chlorella (2053 ± 83 and 983 ± 35 µmol·l-1) (P < 0·001), but were not affected by age (P > 0·05). Postprandial total and essential amino acid availabilities were highest for pea, spirulina and mycoprotein and lowest for chlorella (all P < 0·05), but no effect of age was observed (P > 0·05). The ingestion of a variety of novel non-animal-derived dietary protein sources elicits divergent plasma amino acid responses, which are further modulated by age.

Ingestion of 'whole cell' or 'split cell' Chlorella sp., Arthrospira sp., and milk protein show divergent postprandial plasma amino acid responses with similar postprandial blood glucose control in humans.

Microalgae provide a sustainable basis for protein-rich food production. However, human data concerning microalgae ingestion, subsequent postprandial amino acid (AA) availability and associated metabolic responses are minimal. We investigated ingesting Arthrospira sp. (spirulina;SPR), and Chlorella sp. (chlorella; in 'whole cell' [WCC] and 'split cell' [SCC] forms, the latter proposed to improve digestibility), compared with a high-quality animal derived protein source (milk; MLK). Ten participants (age; 21 ± 1y, BMI; 25 ± 1 kg·m-2) completed a randomised, crossover, double-blind study, partaking in 4 counterbalanced (for order) experimental visits. At each visit participants ingested SPR, WCC, SCC or MLK drinks containing 20 g protein and 75 g carbohydrate. Arterialised venous blood samples, indirect calorimetry and visual analogue scales were assessed postabsorptive, and throughout a 5 h postprandial period to measure AA, glucose, insulin and uric acid concentrations, whole-body energy expenditure and appetite scores, respectively. Protein ingestion increased plasma AA concentrations (p < 0.001) to differing total postprandial total-and essential-AA availabilities; highest for MLK (86.6 ± 17.8 mmol·L-1) and SPR (84.9 ± 12.5 mmol·L-1), lowest for WCC (-4.1 ± 21.7 mmol·L-1; p < 0.05), with SCC (55.7 ± 11.2 mmol·L-1) marginally greater than WCC (p = 0.09). No differences (p > 0.05) were detected between conditions for postprandial glucose or insulin concentrations, whole-body energy expenditure or appetite scores, but serum uric acid concentrations increased (p < 0.05) following microalgae ingestion only. Our data imply that microalgae can present a bioavailable source of protein for human nutrition, however, challenges remain, requiring species selection and/or biomass processing to overcome.

Algae Ingestion Increases Resting and Exercised Myofibrillar Protein Synthesis Rates to a Similar Extent as Mycoprotein in Young Adults

BackgroundSpirulina [SPIR] (cyanobacterium) and chlorella [CHLO] (microalgae) are foods rich in protein and essential amino acids; however, their capacity to stimulate myofibrillar protein synthesis (MyoPS) in humans remains unknown. ObjectivesWe assessed the impact of ingesting SPIR and CHLO compared with an established high-quality nonanimal-derived dietary protein source (fungal-derived mycoprotein [MYCO]) on plasma amino acid concentrations, as well as resting and postexercise MyoPS rates in young adults. MethodsThirty-six healthy young adults (age: 22 ± 3 y; BMI: 23 ± 3 kg·m-2; male [m]/female [f], 18/18) participated in a randomized, double-blind, parallel-group trial. Participants received a primed, continuous infusion of L-[ring-2H5]-phenylalanine and completed a bout of unilateral-resistance leg exercise before ingesting a drink containing 25 g protein from MYCO (n = 12; m/f, 6/6), SPIR (n = 12; m/f, 6/6), or CHLO (n = 12; m/f, 6/6). Blood and bilateral muscle samples were collected at baseline and during a 4-h postprandial and postexercise period to assess the plasma amino acid concentrations and MyoPS rates in rested and exercised tissue. ResultsProtein ingestion increased the plasma total and essential amino acid concentrations (time effects; all P < 0.001), but most rapidly and with higher peak responses following the ingestion of SPIR compared with MYCO and CHLO (P < 0.05), and MYCO compared with CHLO (P < 0.05). Protein ingestion increased MyoPS rates (time effect; P < 0.001) in both rested (MYCO, from 0.041 ± 0.032 to 0.060 ± 0.015%·h−1; SPIR, from 0.042 ± 0.030 to 0.066 ± 0.022%·h−1; and CHLO, from 0.037 ± 0.007 to 0.055 ± 0.019%·h−1, respectively) and exercised tissue (MYCO, from 0.046 ± 0.014 to 0.092 ± 0.024%·h−1; SPIR, from 0.038 ± 0.011 to 0.086 ± 0.028%·h−1; and CHLO, from 0.048 ± 0.019 to 0.090 ± 0.024%·h−1, respectively), with no differences between groups (interaction effect; P > 0.05), but with higher rates in exercised compared with rested muscle (time × exercise effect; P < 0.001). ConclusionsThe ingestion of a single bolus of algae-derived SPIR and CHLO increases resting and postexercise MyoPS rates to a comparable extent as MYCO, despite divergent postprandial plasma amino acid responses.

74 Effects of meal frequency on plasma amino acid concentrations in horses of various body condition scores

Meal frequency affects equine energy metabolism and behavior. However, the effect of meal frequency on amino acid (AA) metabolism has not been investigated in horses, despite plasma AA profiles being explored as indicators of altered metabolism associated with equid disease states. Being either over or underconditioned is often linked with those disease states. The objective of this study was to determine the effect of feeding frequency on plasma AA responses in metabolically healthy horses of various stable body conditions. An oral sugar test was used to screen and exclude horses with insulin dysregulation from use in the study. Horses (n = 12) were selected to include a range of Henneke body condition scores (4–7). Horses were fed to maintain condition with both complimentary feed (0.45% BW DM; 16% CP) and hay (1.55% BW DM; 11% CP; in slow feeder nets) provided at once (1x; 0800 h), split across 2 feedings (2x; 0800 and 1800 h), or split across 3 feedings (3x; 0800, 1300, and 1800 h). After a 14 d adaptation, 2 groups of 6 horses each were randomly allocated to meal frequency regimens. Meal frequency regimens took place for 7 d each in a crossover design. Jugular vein catheters were placed on d 7 of each meal frequency regimen. Blood samples were taken relative to the morning feeding at −30, 0, 30, 60, 90, 120, 180 min. A mixed model with repeated measures in SASwas used to determine the effects of meal frequency, time point, and body condition score on plasma AA concentrations. Complementary feed meals were eaten completely post provision with. minimal hay orts. With the exception of glutamate, all plasma AA concentrations increased after meal consumption (P < 0.01). While meal feeding frequency did affect plasma AA concentrations for most AAs (P < 0.01), there was no interaction between meal frequency and time point for any AA (P > 0.7). Indispensable postprandial plasma AA concentration increases over baseline at 60 min (average ± SE) were 56 ± 7%, 56 ± 8%, and 59 ± 7% for the 1x, 2x, and 3x meal feeding regimens, respectively. This finding demonstrates that even one third of the dietary allotment was able to create increases in plasma AA concentrations similar to the 1x feeding regimen. Feeding smaller more frequent meals could be a simple way to improve protein and AA bioavailability in equine diets. Body condition score affected plasma concentrations of alanine, arginine, aspartate, and tyrosine (P < 0.01). When investigating plasma AA profiles related to disease states, body condition, in addition to diet and fed/fasting state, should be reported as it may affect underlying protein metabolism.

O87 The post-prandial plasma and whole blood amino acid response to consumption of diets with increasing pulse inclusion in adult dogs

O87 The post-prandial plasma and whole blood amino acid response to consumption of diets with increasing pulse inclusion in adult dogs

Whey protein concentrate mixed beverages and plasma amino acid response in young males

Whey protein isolate (WPI) and whey protein hydrolysate (WPH) contains more protein than whey protein concentrate. However, to achieve a better taste, most commercial products mix WPI and WPH with whey protein concentrate (WPC). This study aimed to compare postprandial blood amino acids following ingestion of three beverages: WPImixed with WPC (WPI-mixed), WPH-mixed with WPI (WPH-mixed), and placebo. A total of ten healthy men aged between 18 and 30, who regularly engaged in exercise training, were recruited as participants. They each received 350 mL of each beverage on separate days and 6-day apart. Concentrations of plasma essential amino acids (EAA), branched-chain amino acids (BCAA), and leucine (Leu) were measured in blood samples taken from participants every 15 mins for 2 hrs. Plasma concentrations of EAA, BCAA, and Leu increased after ingestion of the WPI-mixed and WPH-mixed beverages versus the placebo beverage (P&lt;0.05). Plasma EAA did not differ between WPI- mixed and WPmixed trials. In contrast, plasma concentrations of BCAA after WPI-mixed were higher than after WPH-mixed at 30 mins. The same was observed for Leu at 30 and 75 mins after ingestion. The higher plasma BCAA and Leu in the WPI-mixed trial versus the WPHmixed trial may have been due to the presence of short-chain peptides, as bioactive peptides, in WPH-mixed, which were absorbed. In conclusion, there was no difference in plasma EAA, but plasma concentrations of leucine and BCAA were higher in the WPImixed trial than WPH-mixed trial. Therefore, future research should investigate bioactive peptides along with plasma amino acids.

Ingestion of an ample amount of meat substitute based on a lysine-enriched, plant-based protein blend stimulates postprandial muscle protein synthesis to a similar extent as an isonitrogenous amount of chicken in healthy, young men.

Plant-based proteins are considered to be less effective in their capacity to stimulate muscle protein synthesis when compared with animal-based protein sources, likely due to differences in amino acid contents. We compared the postprandial muscle protein synthetic response following the ingestion of a lysine-enriched plant-based protein product with an isonitrogenous amount of chicken. Twenty-four men (age 24 ± 5 years; BMI 22·9 ± 2·6 kg·m-2) participated in this parallel, double-blind, randomised controlled trial and consumed 40 g of protein as a lysine-enriched wheat and chickpea protein product (Plant, n 12) or chicken breast fillet (Chicken, n 12). Primed, continuous intravenous l-(ring-13C6)-phenylalanine infusions were applied while repeated blood and muscle samples were collected over a 5-h postprandial period to assess plasma amino acid responses, muscle protein synthesis rates and muscle anabolic signalling responses. Postprandial plasma leucine and essential amino acid concentrations were higher following Chicken (P < 0·001), while plasma lysine concentrations were higher throughout in Plant (P < 0·001). Total plasma amino acid concentrations did not differ between interventions (P = 0·181). Ingestion of both Plant and Chicken increased muscle protein synthesis rates from post-absorptive: 0·031 ± 0·011 and 0·031 ± 0·013 to postprandial: 0·046 ± 0·010 and 0·055 ± 0·015 % h-1, respectively (P-time < 0·001), with no differences between Plant and Chicken (time x treatment P = 0·068). Ingestion of 40 g of protein in the form of a lysine-enriched plant-based protein product increases muscle protein synthesis rates to a similar extent as an isonitrogenous amount of chicken in healthy, young men. Plant-based protein products sold as meat replacers may be as effective as animal-based protein sources to stimulate postprandial muscle protein synthesis rates in healthy, young individuals.

Plasma Amino Acid Response to Whey Protein Ingestion Following 28 Days of Probiotic (Bacillus subtilis DE111) Supplementation in Active Men and Women.

We sought to determine if 28 days of probiotic supplementation influenced the plasma amino acid (AA) response to acute whey protein feeding. METHODS: Twenty-two recreationally active men (n = 11; 24.3 ± 3.2 yrs; 89.3 ± 7.2 kg) and women (n = 11; 23.0 ± 2.8 yrs; 70.2 ± 15.2 kg) participated in this double-blind, placebo-controlled, randomized study. Before (PRE) and after 28 days of supplementation (POST), participants reported to the lab following a 10-hr fast and provided a resting blood draw (0 min), then subsequently consumed 25 g of whey protein. Blood samples were collected at 15-min intervals for 2 h post-consumption (15–120 min) and later analyzed for plasma leucine, branched-chain AA (BCAA), essential AA (EAA), and total AA (TAA). Participants received a probiotic (PROB) consisting of 1 x10-9 colony forming units (CFU) Bacillus subtilis DE111 (n = 11) or a maltodextrin placebo (PL) (n = 11) for 28 days. Plasma AA response and area under the curve (AUC) values were analyzed via repeated measures analysis of variance. RESULTS: Our analysis indicated no significant (p < 0.05) differential responses for plasma leucine, BCAA, EAA, or TAA between PROB and PL from PRE to POST. AUC analysis revealed no group × time interaction for plasma leucine (p = 0.524), BCAA (p = 0.345), EAA (p = 0.512), and TAA (p = 0.712). CONCLUSION: These data indicate that 28 days of Bacillus subtilis DE111 does not affect plasma AA appearance following acute whey protein ingestion.

The daytime feeding frequency affects appetite-regulating hormones, amino acids, physical activity, and respiratory quotient, but not energy expenditure, in adult cats fed regimens for 21 days.

The effects of feeding frequency on postprandial response of circulating appetite-regulating hormones, insulin, glucose and amino acids, and on physical activity, energy expenditure, and respiratory quotient were studied in healthy adult cats. Two experiments were designed as a 2 x 3 replicated incomplete Latin square design. Eight cats, with an average body weight (BW) of 4.34 kg ± 0.04 and body condition score (BCS) of 5.4 ± 1.4 (9 point scale), were fed isocaloric amounts of a commercial adult maintenance canned cat food either once (0800 h) or four times daily (0800 h, 1130 h, 1500 h, 1830 h). Study 1 consisted of three 21-d periods. On day 14, two fasted and 11 postprandial blood samples were collected over 24 hours to measure plasma concentrations of ghrelin, GLP-1, GIP, leptin, PYY, insulin and amino acids, and whole blood glucose. Physical activity was monitored from day 15 to 21 of each period. In Study 2 indirect calorimetry was performed on the last day of each period. Body weight was measured weekly and feed intake recorded daily in both experiments. No effect of feeding regimen on BW was detected. Cats eating four times daily had lesser plasma concentrations of GIP and GLP-1 (P<0.05) and tended to have lesser plasma PYY concentrations (P<0.1). Plasma leptin and whole blood glucose concentrations did not differ between regimens (P>0.1). Cats fed once daily had a greater postprandial plasma amino acid response, and greater plasma ghrelin and insulin concentrations (P<0.05). Physical activity was greater in cats fed four times (P<0.05), though energy expenditure was similar between treatments at fasting and in postprandial phases. Finally, cats eating one meal had a lower fasting respiratory quotient (P<0.05). Overall, these data indicate that feeding once a day may be a beneficial feeding management strategy for indoor cats to promote satiation and lean body mass.

Casein Protein Processing Strongly Modulates Post-Prandial Plasma Amino Acid Responses In Vivo in Humans.

Micellar casein is characterized as a slowly digestible protein source, and its structure can be modulated by various food processing techniques to modify its functional properties. However, little is known about the impact of such modifications on casein protein digestion and amino acid absorption kinetics and the subsequent post-prandial plasma amino acid responses. In the present study, we determined post-prandial aminoacidemia following ingestion of isonitrogenous amounts of casein protein (40 g) provided as micellar casein (Mi-CAS), calcium caseinate (Ca-CAS), or cross-linked sodium caseinate (XL-CAS). Fifteen healthy, young men (age: 26 ± 4 years, BMI: 23 ± 1 kg·m−2) participated in this randomized cross-over study and ingested 40 g Mi-Cas, Ca-CAS, and XL-CAS protein, with a ~1 week washout between treatments. On each trial day, arterialized blood samples were collected at regular intervals during a 6 h post-prandial period to assess plasma amino acid concentrations using ultra-performance liquid chromatography. Plasma amino acid concentrations were higher following the ingestion of XL-CAS when compared to Mi-CAS and Ca-CAS from t = 15 to 90 min (all p < 0.05). Plasma amino acid concentrations were higher following ingestion of Mi-CAS compared to Ca-CAS from t = 30 to 45 min (both p < 0.05). Plasma total amino acids iAUC were higher following the ingestion of XL-CAS when compared to Ca-CAS (294 ± 63 vs. 260 ± 75 mmol·L−1, p = 0.006), with intermediate values following Mi-CAS ingestion (270 ± 63 mmol·L−1, p > 0.05). In conclusion, cross-linked sodium caseinate is more rapidly digested when compared to micellar casein and calcium caseinate. Protein processing can strongly modulate the post-prandial rise in plasma amino acid bioavailability in vivo in humans.

Metabolic and catecholamine response to sympathetic stimulation in early-treated adult male patients with phenylketonuria

PurposeDefective function of phenylalanine hydroxylase in phenylketonuria (PKU) results in the accumulation of phenylalanine (Phe) and the reduction of tyrosine (Tyr) in the blood, interfering in the normal development and function of organs and tissues in the body. Tyr is the precursor of catecholamines, secreted in response to stress by the adrenal medulla and paraganglia. The aim of this study was to evaluate plasma catecholamine and amino acid response to an escalating series of sympathetic stress tests in PKU patients.MethodsTwelve males with classical PKU (aged 18–41 years) and ten healthy male controls were included in this study. The subjects were exposed to three different sympathetic stress stimulations: cold pressor, isometric handgrip, and peak treadmill tests to exhaustion. Physiological, metabolic, and hormonal changes were determined.ResultsAerobic capacity (VO2max) was significantly lower in the PKU group (p = 0.018); however, relative VO2max was similar in the two groups during the spiroergometric test. No significant differences in norepinephrine or in epinephrine response were found between the two groups during the different stimulation tests. Blood Phe increased significantly in the PKU group compared with controls (p = 0.027) during the spiroergometric test, while Tyr levels remained stable in both groups.ConclusionPKU itself might not influence stress-induced catecholamine changes. Only strenuous exercise increased blood Phe levels in PKU subjects.

Proteins and Amino Acids Treated with Atmospheric Plasma Show Significantly Increased Bioavailability in Humans.

Background:Muscle mass is an important determinant of metabolic health and physical function. It has previously been demonstrated that the postprandial rise in circulating essential amino acids acts as the main stimulus for muscle protein synthesis (MPS). The current study investigated the postprandial plasma essential amino acid (EAA) and branched-chain amino acid (BCAA) responses of (1) Hydrolyzed whey protein isolate (HWPI) compared to plasma treated non-hydrolyzed whey protein isolate (PT-NHWPI), (2) standard branch-chain amino acids (S-BCAA) compared to plasma treated branch-chained amino acids (PT-BCAA), (3) standard pea protein (S-PP), compared to plasma treated pea protein (PT-PP), and (4) HWPI compared to PT-PP.Methods:Ten subjects (24.6 ± 5.3 years; 178.8 ± 8.1 cm; 78.6 ± 10.1 kg) participated in a double-blind, randomized, crossover trial comparing four separate protein conditions (HWPI, PT-NHWPI, S-PP, PT-PP). A separate cohort of ten subjects (26.4 ± 7.4 years; 178.8 ± 5.9 cm; 85 ± 12.3 kg) participated in a double-blind randomized, crossover trial comparing two branch-chain amino acid conditions: S-BCAA and PT-BCAA. All conditions were administered following a 7-day washout. Plasma EAA and BCAA concentrations were assessed from blood donated by subjects at pre-consumption, 30-, 60-, 90-, 120-, and 180 minutes post-consumption.Results:Blood plasma levels of total EAA and BCAA concentration were significantly greater in all treated conditions at 30-, 60-, 90-, and 120 minutes post consumption (P < .05). There were no differences between PT-PP and HWPI.Discussion:All proteins significantly elevated EAAs, and BCAAs from basal levels. However, we conclude that the consumption of the treated proteins significantly raises blood levels of EAAs, and BCAAs to a greater extent across multiple dairy, vegan, and isolated BCAA conditions. Moreover, atmospheric plasma treatment of a vegan protein source makes its amino acid response similar to whey. Thus, protein supplementation with that has undergone Ingredient Optimized® atmospheric plasma treatment technology may be highly beneficial for improving the blood plasma amino acid response.

The glycation level of milk protein strongly modulates post-prandial lysine availability in humans.

Industrial heat treatment of milk results in protein glycation. A high protein glycation level has been suggested to compromise the post-prandial rise in plasma amino acid availability following protein ingestion. In the present study, we assessed the impact of glycation level of milk protein on post-prandial plasma amino acid responses in humans. Fifteen healthy, young men (age 26 (SEM 1) years, BMI 24 (SEM 1) kg/m2) participated in this randomised cross-over study and ingested milk protein powder with protein glycation levels of 3, 20 and 50 % blocked lysine. On each trial day, arterialised blood samples were collected at regular intervals during a 6-h post-prandial period to assess plasma amino acid concentrations using ultra-performance liquid chromatography. Plasma essential amino acid (EAA) concentrations increased following milk protein ingestion, with the 20 and 50 % glycated milk proteins showing lower overall EAA responses compared with the 3 % glycated milk protein (161 (SEM 7) and 142 (SEM 7) v. 178 (SEM 9) mmol/l × 6 h, respectively; P ≤ 0·011). The lower post-prandial plasma amino acid responses were fully attributed to an attenuated post-prandial rise in circulating plasma lysine concentrations. Plasma lysine responses (incremental AUC) following ingestion of the 20 and 50 % glycated milk proteins were 35 (SEM 4) and 92 (SEM 2) % lower compared with the 3 % glycated milk protein (21·3 (SEM 1·4) and 2·8 (SEM 0·7) v. 33·3 (SEM 1·7) mmol/l × 6 h, respectively; P < 0·001). Milk protein glycation lowers post-prandial plasma lysine availability in humans. The lower post-prandial availability of lysine following ingestion of proteins with a high glycation level may compromise the anabolic properties of a protein source.

Females Achieve Higher Plasma Amino Acid Concentrations Than Males After Consuming a 20-gram Whey Protein Supplement but Not a 30-gram Protein Meal (P08-058-19)

ObjectivesWe sought to assess whether there are sex differences in postprandial amino acid (AA) responses to different quantities and sources of dietary protein. MethodsIn a randomized, crossover design, 12 participants [6 males, age: 29 ± 3 y; BMI: 27.1 ± 5.1 kg/m2; mean ± SEM, and 6 females, age: 30 ± 6 y; BMI: 25.0 ± 1.8 kg/m2] completed three 5-h acute feeding trials. They consumed breakfasts containing 10 g of protein from foods (10-PRO), 30 g of protein from foods (30-PRO), and 10 g of protein from foods with an additional 20 g of whey protein isolate (WPI) consumed 120 minutes later (10/20-PRO). Blood samples were collected at times -30, 0, 30, 60, 120, 150, 180, 240, and 300 min relative to breakfast intake. ResultsFor each trial, protein intakes were quantitatively the same for females and males, which resulted in greater protein intakes for females when expressed per kg body mass and liter of plasma volume (Table 1). Plasma AA concentrations did not increase for either sex after 10-PRO (300 min time period) or the first 120 min of 10/20-PRO (before WPI consumed). Plasma total free amino acid (TAA), essential amino acid (EAA), and leucine concentrations (μg/mL) peaked at 240 min for males and at 150, 180, and 240 min respectively, for females, after 30-PRO. TAA, EAA, and leucine concentrations peaked 60 min after consuming 20 g WPI (180 min after breakfast) for 10/20-PRO for both sexes. No differences in composite iAUCpos over 300 min were observed between sexes for 30-PRO. Composite iAUCpos (μg/mL) over 300 min for TAA, EAA, and leucine were greater for females compared to males, by 41, 57, and 40% respectively, for 10/20-PRO. ConclusionsPlasma AA responses to consuming a high-protein breakfast are not different between females and males, but are greater for females after consuming a whey protein supplement. This greater increase in AA concentrations for females may be due to greater rates of absorption and/or a greater quantity of protein intake relative to body mass and plasma volume. Males may require more whey protein than females to achieve comparable plasma AA responses. Funding SourcesPurdue University, Ingestive Behavioral Research Center and Lynn Fellowship to JLH Supporting Tables, Images and/or Graphs▪

Postprandial Plasma Amino Acid Responses Between Standard Whey Protein Isolate and Whey Protein Isolate Plus Novel Technology.

Background:Muscle mass is an important determinant of metabolic health and physical function. It has previously been demonstrated that the postprandial rise in circulating essential amino acids (EAA) acts as the main stimulus for muscle protein synthesis (MPS). This study investigated postprandial plasma amino acid (AA) responses of 2 different forms of whey protein isolate (WPI) with iso-caloric and iso-nitrogenous profiles to investigate plasma concentrations of EAA.Methods:In all, 12 healthy men (n = 12) between 19 and 32 years of age were recruited for a randomized, cross-over design, which involved consumption of protein supplements on 2 testing days separated by a 6-day washout period between conditions. On each testing day, subjects consumed either 29.6 g of WPI or WPI + io (whey protein isolate plus Ingredient Optimized Protein®) mixed with 236 mL of water. Plasma EAA and branch chain amino acid (BCAA) concentrations were assessed from whole body donated by subjects at pre-consumption and 30, 60, 90, 120, and 180 minutes post consumption.Results:Plasma levels of total EAA concentration was significantly greater in WPI + io at 30, 60, 90, and 120 minutes post consumption (P < .01, P < .001, P < .01, and P < .01, respectively). Plasma levels of total BCAA concentration was significantly greater in WPI + io at 30, 60, 90, and 120 minutes post consumption (P < .01, P < .001, P < .01, and P < .05, respectively) compared with WPI. For leucine, only WPI + io had elevated levels compared with pre-test at 90 minutes post consumption (P < .001).Discussion:Both conditions significantly elevated EAA, BCAA, and leucine from basal levels. However, we conclude that the consumption of the treated WPI significantly raises plasma EAA, BCAA, and leucine to a greater extent compared with WPI with no treatment. Thus, supplementation with WPI that has undergone Ingredient Optimized® technology may be highly beneficial for those who partake in regular exercise, elderly individuals, or those affected by a reduced sensitivity to amino acids.

Digestive Responses to Fortified Cow or Goat Dairy Drinks: A Randomised Controlled Trial.

Fortified milk drinks are predominantly manufactured from bovine (cow) sources. Alternative formulations include those prepared with hydrolysed bovine milk proteins or from alternate bovidae species, such as caprine (goat) milk. Currently, there is little data on protein digestive and metabolic responses following ingestion of fortified milk drinks. To examine the digestive and metabolic responses to commercially-available fortified milks, young adults (n = 15 males: 15 females), in a randomised sequence, ingested isonitrogenous quantities of whole cow-protein (WC), whole goat-protein (WG), or partially-hydrolysed whey cow-protein (HC), commercial fortified milks. Plasma amino acid (AA) and hormonal responses were measured at baseline and again at 5 h after ingestion. Paracetamol recovery, breath hydrogen, and subjective digestive responses were also measured. Postprandial plasma AA was similar between WC and WG, while AA appearance was suppressed with HC. Following HC, there was a negative incremental AUC in plasma branched-chain AAs. Further, HC had delayed gastric emptying, increased transit time, and led to exaggerated insulin and GLP-1 responses, in comparison to whole protein formulas. Overall, WC and WG had similar protein and digestive responses with no differences in digestive comfort. Contrastingly, HC led to delayed gastric emptying, attenuated AA appearance, and a heightened circulating insulin response.

Effects of grain species, genotype and starch quantity on the postprandial plasma amino acid response in horses

Postprandial alterations of plasma amino acid (PAA) levels partly reflect a temporal contribution of the feed. How cereal grains affect PAA levels is not known. We hypothesized that a meal of cereal grains causes a temporal increase of PAA, affected by grain species, grain genotype and meal size. Six mares were used in three consecutive trials, receiving four oats, barley and maize genotypes, respectively. Individual grain genotypes were provided as 3 meal sizes corresponding to 1.0, 1.5 or 2.0 g starch/kg body weight. Meadow hay (1.5 kg/100 kg body weight) was offered daily. At the test days, 1 kg hay was fed 60 min prior to the grain meal. Blood samples were taken before grain feeding (0 min) and 30, 60, 90, 120, 180, 240 and 300 min thereafter. Subsequently, the remaining hay was offered. The genotype × starch quantity (i.e., meal size) interaction had a major effect on postprandial PAA concentrations (P < 0.05). Availability of amino acids (AA), ingested from different grain genotypes, apparently differed at both the digestive and post-digestive level. Thus, AA supply from grain feeding can better be assessed on the genotype level. The concentrations of most PAA increased rapidly with a postprandial maximum at around 30 min. Hay feeding might have an underrated capability for AA provision because increases of PAA levels were initialized already by ingestion of a 1 kg hay. It remains unclear which portion of the PAA kinetics response originates from hay feeding and which one from the cereal grain meal.

Plasma Amino Acid, Glucose and Insulin Response to a Metered Intake of Milk or Carbohydrate‐Electrolyte Solution during 5 h Recovery from Exercise in Healthy Active Young Men

Plasma Amino Acid, Glucose and Insulin Response to a Metered Intake of Milk or Carbohydrate‐Electrolyte Solution during 5 h Recovery from Exercise in Healthy Active Young Men