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

2020 ◽  
Vol 6 (1) ◽  
pp. 1
Author(s):  
Jeremy R. Townsend ◽  
William C. Vantrease ◽  
Megan D. Jones ◽  
Philip A. Sapp ◽  
Kent D. Johnson ◽  
...  

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.

Sports ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 13 ◽  
Author(s):  
Jeremy R. Townsend ◽  
Jaclyn E. Morimune ◽  
Megan D. Jones ◽  
Cheryle N. Beuning ◽  
Allison A. Haase ◽  
...  

This double-blind study examined effects of a protease enzyme blend (Prohydrolase®) added to whey protein on post-resistance exercise aminoacidemia and intramuscular anabolic signaling were investigated in ten resistance-trained males. Participants completed 4 sets of 8–10 repetitions in the leg press and leg extension exercises at 75% of 1-repetition maximum. Participants then consumed either 250 mg of Prohydrolase® + 26 g of whey protein (PW), 26 g whey alone (W), or non-nutritive control (CON) in counterbalanced order. Blood samples were obtained prior to exercise (baseline) and then immediately-post (IP), 30-, 60-, 90-, 120-, and 180-min post-exercise. Muscle biopsies were taken at baseline, 1-h (1H), and 3-h (3H) post-exercise. Phosphorylation of AKTSer437 was decreased (3H only: p < 0.001), mTORSer2448 was increased (1H: p = 0.025; 3H: p = 0.009), and p70S6KThr412 remained unchanged similarly for each condition. Plasma leucine, branch-chained amino acids, and essential amino acid concentrations for PW were significantly higher than CON (p < 0.05) at 30 min and similar to W. Compared to IP, PW was the only treatment with elevated plasma leucine levels at 30 min (p = 0.007; ∆ = 57.8 mmol/L, 95% Confidence Interval (CI): 20.0, 95.6) and EAA levels at 180 min (p = 0.003; ∆ = 179.1 mmol/L, 95% CI: 77.5, 280.7). Area under the curve amino acid analysis revealed no differences between PW and W. While no different than W, these data indicate that PW was the only group to produce elevated amino acid concentrations 30-min and 180-min post-ingestion.


2019 ◽  
Vol 3 (Supplement_1) ◽  
Author(s):  
Jessica Brennan ◽  
Maneephan Keerati-U-Rai ◽  
Huaixia Yin ◽  
Julie Daoust ◽  
Emilie Nonnotte ◽  
...  

Abstract Objectives This study assessed the blood essential amino acid (eAA) response after consumption of high quality (PDCAAS = 1.0) plant-based protein blends versus whey protein (WPI, control) in healthy, resistance-trained adult men. Secondary Objectives assessed the blood leucine response (Cmax and Tmax). Methods The study was an acute, randomized, double-blind cross-over study. Participants consumed one of four study products: Blend 1 (34 grams of pea and pumpkin protein); Blend 2 (33 grams of pea, pumpkin, sunflower and coconut protein); Blend 3 (hydrolyzed version of Blend 1). Leucine was matched at 2.6 grams across test beverages equal to WPI (24 grams protein). Total eAA content was 12 grams across beverages. Fasting blood was collected and samples at 15 min, 30 min, 1 h, 2 h, 3 h and 4 h post consumption. Blood eAA were measured by UPLC. Repeated measures ANOVA assessed for equivalence of the total sum of blood eAA concentration. Primary endpoint was iAUC over 4 hours after consumption of the study blends. Cmax and Tmax of blood leucine response were secondary outcomes. Results Eighteen men (25.4 ± 4.64 y) with a BMI of 24.4 ±3.35 kg.m−2 completed the study. The eAA iAUC over 4 hours of plant-based protein blends were not equivalent to WPI, the three ratios [90% CI]: Blend #1: 0.66 [0.58–0.76]; Blend #2: 0.71 [0.62–0.82], Blend #3: 0.60 [0.52–0.69] fell below the pre-defined equivalence threshold [0.80–1.25], indicative of a 30 to 40% decrease compared to WPI. Leucine Cmax over 4-hours of plant-based protein blends were not equivalent to WPI Blend #1: 0.70 [0.67–0.73]; Blend #2: 0.72 [0.68–0.75], Blend #3: 0.65 [0.62–0.68], indicative of a 28 to 35% decrease compared to WPI. Leucine Tmax for Blend #1 and Blend #3 were close to WPI (Blend #1: 0.94 [0.73–1.18]; Blend #2: 1.56 [1.28–1.92]; Blend #3: 1.19 [0.95–1.48]). Conclusions This study represents the first human investigation in which blood eAA responses to high-quality, plant protein blends were compared to WPI. Although the eAA iAUC were not equivalent between plant protein blends and whey control, the leucine kinetic data across our plant protein blends showed an ∼2-fold increase from fasting. Further, similar Tmax data across two plant protein blends suggest a rapid hyperleucinemia. Future studies should assess the impact of high-quality plant proteins on muscle protein synthesis. Funding Sources Sequel Naturals, Danone Research.


Nutrients ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1543 ◽  
Author(s):  
Naomi Yoshii ◽  
Koji Sato ◽  
Riki Ogasawara ◽  
Yusuke Nishimura ◽  
Yasushi Shinohara ◽  
...  

Dietary protein intake is critical for the maintenance of skeletal muscle mass. Plasma amino acid concentrations increase with protein intake and increases in muscle protein synthesis are dependent on leucine concentrations. We aimed to investigate the effect of a mixed meal and free amino acids intake on plasma leucine concentrations. In this randomized crossover study, 10 healthy young men (age 25 ± 1 years, height 1.73 ± 0.02 m, weight 65.8 ± 1.5 kg) underwent tests under different conditions—intake of 2 g of leucine (LEU), intake of a mixed meal (protein 27.5 g, including 2.15 g of leucine, protein: fat: carbohydrate ratio—22:25:53) only (MEAL), intake of 2 g of leucine immediately after a mixed meal (MEAL-LEU) and intake of 2 g of leucine 180 min after a mixed meal (MEAL-LEU180). Blood samples were collected within 420 min (240 min for LEU only) after intake and changes in amino acid concentrations were evaluated. Although the maximum plasma leucine concentration increased to 442 ± 24 µM for LEU, it was lower at 347 ± 16 µM (p < 0.05 vs. LEU) for MEAL-LEU, 205 ± 8 µM (p < 0.05 vs. LEU) for MEAL. The maximum plasma leucine concentration for MEAL-LEU180 increased to 481 ± 27 µM and compared to LEU there was no significant difference (p > 0.1). The observation that rapid elevations in plasma leucine concentrations are suppressed when leucine is ingested at the same time as a meal suggests that the timing of its intake must be considered to maximize the anabolic response.


Sports ◽  
2018 ◽  
Vol 6 (3) ◽  
pp. 70 ◽  
Author(s):  
Jeremy Townsend ◽  
David Bender ◽  
William Vantrease ◽  
Philip Sapp ◽  
Ann Toy ◽  
...  

We sought to determine the effects of probiotic supplementation (Bacillus subtilis DE111; 1 billion CFU∙d−1) on markers of immune and hormonal status in collegiate male athletes following 12 weeks of offseason training. Twenty-five Division I male baseball athletes (20.1 ± 1.5 years, 85.5 ± 10.5 kg, 184.7 ± 6.3 cm) participated in this double blind, placebo-controlled, randomized study. Participants were randomly assigned to a probiotic (PRO; n = 13) or placebo (PL; n = 12) group. Pre- and post-training, all athletes provided resting blood and saliva samples. Circulating concentrations of testosterone, cortisol, TNF-α, IL-10, and zonulin were examined in the blood, while salivary immunoglobulin A (SIgA) and SIgM were assayed as indicators of mucosal immunity. Separate analyses of covariance (ANCOVA) were performed on all measures collected post intervention. No differences in measures of body composition or physical performance were seen between groups. TNF-α concentrations were significantly (p = 0.024) lower in PRO compared to PL, while there were no significant group differences in any other biochemical markers examined. A main effect for time was observed (p < 0.05) for increased testosterone (p = 0.045), IL-10 (p = 0.048), SIgA rate (p = 0.031), and SIgM rate (p = 0.002) following offseason training. These data indicate that probiotic supplementation had no effect on body composition, performance, hormonal status, or gut permeability, while it may attenuate circulating TNF-α in athletes.


1990 ◽  
Vol 258 (1) ◽  
pp. E117-E125 ◽  
Author(s):  
P. Castellino ◽  
L. Luzi ◽  
S. Del Prato ◽  
R. A. DeFronzo

The separate and combined effects of insulin and epinephrine on leucine metabolism were examined in healthy young volunteers. Subjects participated in four experimental protocols: 1) euglycemic insulin clamp (+80 microU/ml), 2) epinephrine infusion (50 ng.kg-1.min-1) plus somatostatin with basal replacement of insulin and glucagon, 3) combined epinephrine (50 ng.kg-1.min-1) plus insulin (+80 microU/ml) infusion, and 4) epinephrine and somatostatin as in study 2 plus basal amino acid replacement. Studies were performed with a prime-continuous infusion of [1-14C]leucine and indirect calorimetry. Our results indicate that 1) hyperinsulinemia causes a generalized decrease in plasma amino acid concentrations, including leucine; 2) the reduction in plasma leucine concentration is primarily due to an inhibition of endogenous leucine flux; nonoxidative leucine disposal decreases after insulin infusion; 3) epinephrine, without change in plasma insulin concentration, reduces plasma amino acid levels; 4) combined epinephrine-insulin infusion causes a greater decrease in plasma amino levels than observed with either hormone alone; this is because of a greater inhibition of endogenous leucine flux; and 5) when basal amino acid concentrations are maintained constant with a balanced amino acid infusion, epinephrine inhibits the endogenous leucine flux. In conclusion, the present results do not provide support for the concept that epinephrine is a catabolic hormone with respect to amino acid-protein metabolism. In contrast, epinephrine markedly inhibits insulin-mediated glucose metabolism.


2011 ◽  
Vol 31 (5) ◽  
pp. 1321-1333 ◽  
Author(s):  
Najmeh Khalili-Mahani ◽  
Matthias JP van Osch ◽  
Evelinda Baerends ◽  
Roelof P Soeter ◽  
Marieke de Kam ◽  
...  

We have examined sensitivity and specificity of pseudocontinuous arterial spin labeling (PCASL) to detect global and regional changes in cerebral blood flow (CBF) in response to two different psychoactive drugs. We tested alcohol and morphine in a placebo-controlled, double-blind randomized study in 12 healthy young men. Drugs were administered intravenously. Validated pharmacokinetic protocols achieved minimal intersubject and intrasubject variance in plasma drug concentration. Permutation-based statistical testing of a mixed effect repeated measures model revealed a widespread increase in absolute CBF because of both morphine and alcohol. Conjunction analysis revealed overlapping effects of morphine and alcohol on absolute CBF in the left anterior cingulate, right hippocampus, right insula, and left primary sensorimotor areas. Effects of morphine and alcohol on relative CBF (obtained from z-normalization of absolute CBF maps) were significantly different in the left putamen, left frontoparietal network, cerebellum, and the brainstem. Corroborating previous PET results, our findings suggest that PCASL is a promising tool for central nervous system drug research.


2019 ◽  
Vol 123 (5) ◽  
pp. 545-552 ◽  
Author(s):  
Jean Nyakayiru ◽  
Glenn A. A. van Lieshout ◽  
Jorn Trommelen ◽  
Janneau van Kranenburg ◽  
Lex B. Verdijk ◽  
...  

AbstractIndustrial 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.


2006 ◽  
Vol 38 (Supplement) ◽  
pp. S113
Author(s):  
Douglas Paddon-Jones ◽  
Brock Symons ◽  
Tara L. Cocke ◽  
Scott E. Schutzler ◽  
Arny A. Ferrando ◽  
...  

2013 ◽  
Vol 21 (3) ◽  
pp. 164-171 ◽  
Author(s):  
Luis Vitetta ◽  
Samantha Coulson ◽  
Shoshannah L. Beck ◽  
Helen Gramotnev ◽  
Sharon Du ◽  
...  

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