Publications by year
2023
van der Heijden I, West S, Monteyne AJ, Finnigan TJA, Abdelrahman DR, Murton AJ, Stephens FB, Wall BT (2023). Algae Ingestion Increases Resting and Exercised Myofibrillar Protein Synthesis Rates to a Similar Extent as Mycoprotein in Young Adults.
J Nutr,
153(12), 3406-3417.
Abstract:
Algae Ingestion Increases Resting and Exercised Myofibrillar Protein Synthesis Rates to a Similar Extent as Mycoprotein in Young Adults.
BACKGROUND: Spirulina [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. OBJECTIVES: We 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. METHODS: Thirty-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. RESULTS: Protein 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). CONCLUSIONS: the 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.
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van der Heijden I, Monteyne AJ, Stephens FB, Wall BT (2023). Alternative dietary protein sources to support healthy and active skeletal muscle aging.
Nutr Rev,
81(2), 206-230.
Abstract:
Alternative dietary protein sources to support healthy and active skeletal muscle aging.
To mitigate the age-related decline in skeletal muscle quantity and quality, and the associated negative health outcomes, it has been proposed that dietary protein recommendations for older adults should be increased alongside an active lifestyle and/or structured exercise training. Concomitantly, there are growing environmental concerns associated with the production of animal-based dietary protein sources. The question therefore arises as to where this dietary protein required for meeting the protein demands of the rapidly aging global population should (or could) be obtained. Various non-animal-derived protein sources possess favorable sustainability credentials, though much less is known (compared with animal-derived proteins) about their ability to influence muscle anabolism. It is also likely that the anabolic potential of various alternative protein sources varies markedly, with the majority of options remaining to be investigated. The purpose of this review was to thoroughly assess the current evidence base for the utility of alternative protein sources (plants, fungi, insects, algae, and lab-grown "meat") to support muscle anabolism in (active) older adults. The solid existing data portfolio requires considerable expansion to encompass the strategic evaluation of the various types of dietary protein sources. Such data will ultimately be necessary to support desirable alterations and refinements in nutritional guidelines to support healthy and active aging, while concomitantly securing a sustainable food future.
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Wilkinson K, Koscien CP, Monteyne AJ, Wall BT, Stephens FB (2023). Association of postprandial postexercise muscle protein synthesis rates with dietary leucine: a systematic review.
Physiol Rep,
11(15).
Abstract:
Association of postprandial postexercise muscle protein synthesis rates with dietary leucine: a systematic review.
BACKGROUND: Dietary protein ingestion augments post (resistance) exercise muscle protein synthesis (MPS) rates. It is thought that the dose of leucine ingested within the protein (leucine threshold hypothesis) and the subsequent plasma leucine variables (leucine trigger hypothesis; peak magnitude, rate of rise, and total availability) determine the magnitude of the postprandial postexercise MPS response. METHODS: a quantitative systematic review was performed extracting data from studies that recruited healthy adults, applied a bout of resistance exercise, ingested a bolus of protein within an hour of exercise, and measured plasma leucine concentrations and MPS rates (delta change from basal). RESULTS: Ingested leucine dose was associated with the magnitude of the MPS response in older, but not younger, adults over acute (0-2 h, r2 = 0.64, p = 0.02) and the entire postprandial (>2 h, r2 = 0.18, p = 0.01) period. However, no single plasma leucine variable possessed substantial predictive capacity over the magnitude of MPS rates in younger or older adults. CONCLUSION: Our data provide support that leucine dose provides predictive capacity over postprandial postexercise MPS responses in older adults. However, no threshold in older adults and no plasma leucine variable was correlated with the magnitude of the postexercise anabolic response.
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West S, Monteyne AJ, Whelehan G, van der Heijden I, Abdelrahman DR, Murton AJ, Finnigan TJA, Stephens FB, Wall BT (2023). Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals.
Am J Physiol Endocrinol Metab,
325(3), E267-E279.
Abstract:
Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals.
Pea protein is an attractive nonanimal-derived protein source to support dietary protein requirements. However, although high in leucine, a low methionine content has been suggested to limit its anabolic potential. Mycoprotein has a complete amino acid profile which, at least in part, may explain its ability to robustly stimulate myofibrillar protein synthesis (MyoPS) rates. We hypothesized that an inferior postexercise MyoPS response would be seen following ingestion of pea protein compared with mycoprotein, which would be (partially) rescued by blending the two sources. Thirty-three healthy, young [age: 21 ± 1 yr, body mass index (BMI): 24 ± 1 kg·m-2] and resistance-trained participants received primed, continuous infusions of l-[ring-2H5]phenylalanine and completed a bout of whole body resistance exercise before ingesting 25 g of protein from mycoprotein (MYC, n = 11), pea protein (PEA, n = 11), or a blend (39% MYC, 61% PEA) of the two (BLEND, n = 11). Blood and muscle samples were taken pre-, 2 h, and 4 h postexercise/protein ingestion to assess postabsorptive and postprandial postexercise myofibrillar protein fractional synthetic rates (FSRs). Protein ingestion increased plasma essential amino acid and leucine concentrations (time effect; P < 0.0001), but more rapidly in BLEND and PEA compared with MYC (time × condition interaction; P < 0.0001). From similar postabsorptive values (MYC, 0.026 ± 0.008%·h-1; PEA, 0.028 ± 0.007%·h-1; BLEND, 0.026 ± 0.006%·h-1), resistance exercise and protein ingestion increased myofibrillar FSRs (time effect; P < 0.0001) over a 4-h postprandial period (MYC, 0.076 ± 0.004%·h-1; PEA, 0.087 ± 0.01%·h-1; BLEND, 0.085 ± 0.01%·h-1), with no differences between groups (all; P > 0.05). These data show that all three nonanimal-derived protein sources have utility in supporting postexercise muscle reconditioning.NEW & NOTEWORTHY This study provides evidence that pea protein (PEA), mycoprotein (MYC), and their blend (BLEND) can support postexercise myofibrillar protein synthesis rates following a bout of whole body resistance exercise. Furthermore, these data suggest that a methionine deficiency in pea may not limit its capacity to stimulate an acute increase in muscle protein synthesis (MPS).
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West S, Monteyne AJ, Whelehan G, Abdelrahman DR, Murton AJ, Finnigan TJA, Blackwell JR, Stephens FB, Wall BT (2023). Mycoprotein ingestion within or without its wholefood matrix results in equivalent stimulation of myofibrillar protein synthesis rates in resting and exercised muscle of young men.
Br J Nutr,
130(1), 20-32.
Abstract:
Mycoprotein ingestion within or without its wholefood matrix results in equivalent stimulation of myofibrillar protein synthesis rates in resting and exercised muscle of young men.
Ingestion of mycoprotein stimulates skeletal muscle protein synthesis (MPS) rates to a greater extent than concentrated milk protein when matched for leucine content, potentially attributable to the wholefood nature of mycoprotein. We hypothesised that bolus ingestion of mycoprotein as part of its wholefood matrix would stimulate MPS rates to a greater extent compared with a leucine-matched bolus of protein concentrated from mycoprotein. Twenty-four healthy young (age, 21 ± 2 years; BMI, 24 ± 3 kg.m2) males received primed, continuous infusions of L-[ring-2H5]phenylalanine and completed a bout of unilateral resistance leg exercise before ingesting either 70 g mycoprotein (MYC; 31·4 g protein, 2·5 g leucine; n 12) or 38·2 g of a protein concentrate obtained from mycoprotein (PCM; 28·0 g protein, 2·5 g leucine; n 12). Blood and muscle samples (vastus lateralis) were taken pre- and (4 h) post-exercise/protein ingestion to assess postabsorptive and postprandial myofibrillar protein fractional synthetic rates (FSR) in resting and exercised muscle. Protein ingestion increased plasma essential amino acid and leucine concentrations (P < 0·0001), but more rapidly (both 60 v. 90 min; P < 0·0001) and to greater magnitudes (1367 v. 1346 μmol·l-1 and 298 v. 283 μmol·l-1, respectively; P < 0·0001) in PCM compared with MYC. Protein ingestion increased myofibrillar FSR (P < 0·0001) in both rested (MYC, Δ0·031 ± 0·007 %·h-1 and PCM, Δ0·020 ± 0·008 %·h-1) and exercised (MYC, Δ0·057 ± 0·011 %·h-1 and PCM, Δ0·058 ± 0·012 %·h-1) muscle, with no differences between conditions (P > 0·05). Mycoprotein ingestion results in equivalent postprandial stimulation of resting and post-exercise myofibrillar protein synthesis rates irrespective of whether it is consumed within or without its wholefood matrix.
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West S, Monteyne AJ, van der Heijden I, Stephens FB, Wall BT (2023). Nutritional Considerations for the Vegan Athlete.
Adv Nutr,
14(4), 774-795.
Abstract:
Nutritional Considerations for the Vegan Athlete.
Accepting a continued rise in the prevalence of vegan-type diets in the general population is also likely to occur in athletic populations, it is of importance to assess the potential impact on athletic performance, adaptation, and recovery. Nutritional consideration for the athlete requires optimization of energy, macronutrient, and micronutrient intakes, and potentially the judicious selection of dietary supplements, all specified to meet the individual athlete's training and performance goals. The purpose of this review is to assess whether adopting a vegan diet is likely to impinge on such optimal nutrition and, where so, consider evidence based yet practical and pragmatic nutritional recommendations. Current evidence does not support that a vegan-type diet will enhance performance, adaptation, or recovery in athletes, but equally suggests that an athlete can follow a (more) vegan diet without detriment. A clear caveat, however, is that vegan diets consumed spontaneously may induce suboptimal intakes of key nutrients, most notably quantity and/or quality of dietary protein and specific micronutrients (eg, iron, calcium, vitamin B12, and vitamin D). As such, optimal vegan sports nutrition requires (more) careful consideration, evaluation, and planning. Individual/seasonal goals, training modalities, athlete type, and sensory/cultural/ethical preferences, among other factors, should all be considered when planning and adopting a vegan diet.
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Monteyne AJ, Coelho MOC, Murton AJ, Abdelrahman DR, Blackwell JR, Koscien CP, Knapp KM, Fulford J, Finnigan TJA, Dirks ML, et al (2023). Vegan and Omnivorous High Protein Diets Support Comparable Daily Myofibrillar Protein Synthesis Rates and Skeletal Muscle Hypertrophy in Young Adults.
J Nutr,
153(6), 1680-1695.
Abstract:
Vegan and Omnivorous High Protein Diets Support Comparable Daily Myofibrillar Protein Synthesis Rates and Skeletal Muscle Hypertrophy in Young Adults.
BACKGROUND: it remains unclear whether non-animal-derived dietary protein sources (and therefore vegan diets) can support resistance training-induced skeletal muscle remodeling to the same extent as animal-derived protein sources. METHODS: in Phase 1, 16 healthy young adults (m = 8, f = 8; age: 23 ± 1 y; BMI: 23 ± 1 kg/m2) completed a 3-d dietary intervention (high protein, 1.8 g·kg bm-1·d-1) where protein was derived from omnivorous (OMNI1; n = 8) or exclusively non-animal (VEG1; n = 8) sources, alongside daily unilateral leg resistance exercise. Resting and exercised daily myofibrillar protein synthesis (MyoPS) rates were assessed using deuterium oxide. In Phase 2, 22 healthy young adults (m = 11, f = 11; age: 24 ± 1 y; BMI: 23 ± 0 kg/m2) completed a 10 wk, high-volume (5 d/wk), progressive resistance exercise program while consuming an omnivorous (OMNI2; n = 12) or non-animal-derived (VEG2; n = 10) high-protein diet (∼2 g·kg bm-1·d-1). Muscle fiber cross-sectional area (CSA), whole-body lean mass (via DXA), thigh muscle volume (via MRI), muscle strength, and muscle function were determined pre, after 2 and 5 wk, and postintervention. OBJECTIVES: to investigate whether a high-protein, mycoprotein-rich, non-animal-derived diet can support resistance training-induced skeletal muscle remodeling to the same extent as an isonitrogenous omnivorous diet. RESULTS: Daily MyoPS rates were ∼12% higher in the exercised than in the rested leg (2.46 ± 0.27%·d-1 compared with 2.20 ± 0.33%·d-1 and 2.62 ± 0.56%·d-1 compared with 2.36 ± 0.53%·d-1 in OMNI1 and VEG1, respectively; P < 0.001) and not different between groups (P > 0.05). Resistance training increased lean mass in both groups by a similar magnitude (OMNI2 2.6 ± 1.1 kg, VEG2 3.1 ± 2.5 kg; P > 0.05). Likewise, training comparably increased thigh muscle volume (OMNI2 8.3 ± 3.6%, VEG2 8.3 ± 4.1%; P > 0.05), and muscle fiber CSA (OMNI2 33 ± 24%, VEG2 32 ± 48%; P > 0.05). Both groups increased strength (1 repetition maximum) of multiple muscle groups, to comparable degrees. CONCLUSIONS: Omnivorous and vegan diets can support comparable rested and exercised daily MyoPS rates in healthy young adults consuming a high-protein diet. This translates to similar skeletal muscle adaptive responses during prolonged high-volume resistance training, irrespective of dietary protein provenance. This trial was registered at clinicaltrials.gov as NCT03572127.
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2022
Coelho MOC, Monteyne AJ, Kamalanathan ID, Najdanovic-Visak V, Finnigan TJA, Stephens FB, Wall BT (2022). High dietary nucleotide consumption for one week increases circulating uric acid concentrations but does not compromise metabolic health: a randomised controlled trial.
Clinical Nutrition ESPEN,
49, 40-52.
Abstract:
High dietary nucleotide consumption for one week increases circulating uric acid concentrations but does not compromise metabolic health: a randomised controlled trial
Background & aims: Elevated circulating uric acid concentrations have been linked to various cardio-metabolic diseases. Bolus consumption of a nucleotide-rich dietary protein source increases postprandial serum uric acid concentrations. We assessed the impact of twice-daily nucleotide-rich mixed-meal consumption for one week on postabsorptive serum uric acid concentrations, insulin sensitivity (IS), glycaemic control and the plasma lipidome. Methods: Twenty healthy adults participated in a randomised, controlled, parallel-group trial in which they consumed a 7 d fully-controlled eucaloric diet where lunch and dinner contained either nucleotide-depleted (LOW) or high-nucleotide (HIGH) mycoprotein. Postabsorptive blood samples were obtained pre, throughout and post-intervention, and oral glucose tolerance tests were performed pre- and post-intervention. Daily waking urine samples and 24 h continuous blood glucose measurements were collected throughout. Results: Postabsorptive serum uric acid concentrations remained unchanged in LOW but increased throughout the intervention week in HIGH (from 295 ± 17 to 472 ± 29 μmol L−1 by day 6; P < 0.05). Urinary uric acid did not change throughout the intervention in either group. The intervention did not affect indices of IS, 24 h glycaemic control, nor had a meaningful impact on the plasma lipidome. Conclusions: One week of twice-daily consumption of nucleotide-rich mixed-meals increases postabsorptive serum uric acid concentrations above clinically acceptable thresholds but these changes are not associated with deleterious effects on IS, daily glycaemic control or plasma lipid composition. Clinical trial registry: NCT02984358 (https://clinicaltrials.gov/ct2/show/NCT02984358).
Abstract.
2021
Monteyne AJ, Dunlop MV, Machin DJ, Coelho MOC, Pavis GF, Porter C, Murton AJ, Abdelrahman DR, Dirks ML, Stephens FB, et al (2021). A mycoprotein-based high-protein vegan diet supports equivalent daily myofibrillar protein synthesis rates compared with an isonitrogenous omnivorous diet in older adults: a randomised controlled trial.
Br J Nutr,
126(5), 674-684.
Abstract:
A mycoprotein-based high-protein vegan diet supports equivalent daily myofibrillar protein synthesis rates compared with an isonitrogenous omnivorous diet in older adults: a randomised controlled trial.
Animal-derived dietary protein ingestion and physical activity stimulate myofibrillar protein synthesis rates in older adults. We determined whether a non-animal-derived diet can support daily myofibrillar protein synthesis rates to the same extent as an omnivorous diet. Nineteen healthy older adults (aged 66 (sem 1) years; BMI 24 (sem 1) kg/m2; twelve males, seven females) participated in a randomised, parallel-group, controlled trial during which they consumed a 3-d isoenergetic high-protein (1·8 g/kg body mass per d) diet, where the protein was provided from predominantly (71 %) animal (OMNI; n 9; six males, three females) or exclusively vegan (VEG; n 10; six males, four females; mycoprotein providing 57 % of daily protein intake) sources. During the dietary control period, participants conducted a daily bout of unilateral resistance-type leg extension exercise. Before the dietary control period, participants ingested 400 ml of deuterated water, with 50-ml doses consumed daily thereafter. Saliva samples were collected throughout to determine body water 2H enrichments, and muscle samples were collected from rested and exercised muscle to determine daily myofibrillar protein synthesis rates. Deuterated water dosing resulted in body water 2H enrichments of approximately 0·78 (sem 0·03) %. Daily myofibrillar protein synthesis rates were 13 (sem 8) (P = 0·169) and 12 (sem 4) % (P = 0·016) greater in the exercised compared with rested leg (1·59 (sem 0·12) v. 1·77 (sem 0·12) and 1·76 (sem 0·14) v. 1·93 (sem 0·12) %/d) in OMNI and VEG groups, respectively. Daily myofibrillar protein synthesis rates did not differ between OMNI and VEG in either rested or exercised muscle (P > 0·05). Over the course of a 3-d intervention, omnivorous- or vegan-derived dietary protein sources can support equivalent rested and exercised daily myofibrillar protein synthesis rates in healthy older adults consuming a high-protein diet.
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Coelho MOC, Monteyne AJ, Dirks ML, Finnigan TJA, Stephens FB, Wall BT (2021). Daily mycoprotein consumption for 1 week does not affect insulin sensitivity or glycaemic control but modulates the plasma lipidome in healthy adults: a randomised controlled trial.
Br J Nutr,
125(2), 147-160.
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Daily mycoprotein consumption for 1 week does not affect insulin sensitivity or glycaemic control but modulates the plasma lipidome in healthy adults: a randomised controlled trial.
Mycoprotein consumption has been shown to improve acute postprandial glycaemic control and decrease circulating cholesterol concentrations. We investigated the impact of incorporating mycoprotein into the diet on insulin sensitivity (IS), glycaemic control and plasma lipoprotein composition. Twenty healthy adults participated in a randomised, parallel-group trial in which they consumed a 7 d fully controlled diet where lunch and dinner contained either meat/fish (control group, CON) or mycoprotein (MYC) as the primary source of dietary protein. Oral glucose tolerance tests were performed pre- and post-intervention, and 24 h continuous blood glucose monitoring was applied throughout. Fasting plasma samples were obtained pre- and post-intervention and were analysed using quantitative, targeted NMR-based metabonomics. There were no changes within or between groups in blood glucose or serum insulin responses, nor in IS or 24 h glycaemic profiles. No differences between groups were found for 171 of the 224 metabonomic targets. Forty-five lipid concentrations of different lipoprotein fractions (VLDL, LDL, intermediate-density lipoprotein and HDL) remained unchanged in CON but showed a coordinated decrease (7-27 %; all P < 0·05) in MYC. Total plasma cholesterol, free cholesterol, LDL-cholesterol, HDL2-cholesterol, DHA and n-3 fatty acids decreased to a larger degree in MYC (14-19 %) compared with CON (3-11 %; P < 0·05). Substituting meat/fish for mycoprotein twice daily for 1 week did not modulate whole-body IS or glycaemic control but resulted in changes to plasma lipid composition, the latter primarily consisting of a coordinated reduction in circulating cholesterol-containing lipoproteins.
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2020
Davenport AD, Jameson TSO, Kilroe SP, Monteyne AJ, Pavis GF, Wall BT, Dirks ML, Alamdari N, Mikus CR, Stephens FB, et al (2020). A Randomised, Placebo-Controlled, Crossover Study Investigating the Optimal Timing of a Caffeine-Containing Supplement for Exercise Performance.
Sports Med Open,
6(1).
Abstract:
A Randomised, Placebo-Controlled, Crossover Study Investigating the Optimal Timing of a Caffeine-Containing Supplement for Exercise Performance.
BACKGROUND: Pre-exercise supplements containing low doses of caffeine improve endurance exercise performance, but the most efficacious time for consumption before intense endurance exercise remains unclear, as does the contribution of caffeine metabolism. METHODS: This study assessed the timing of a commercially available supplement containing 200 mg of caffeine, 1600 mg of β-alanine and 1000 mg of quercetin [Beachbody Performance Energize, Beachbody LLC, USA] on exercise performance, perception of effort and plasma caffeine metabolites. Thirteen cyclists (V̇O2max 64.5 ± 1.4 ml kg- 1 min- 1 (± SEM)) completed four experimental visits consisting of 30 min of steady-state exercise on a cycle ergometer at 83 ± 1% V̇O2max followed by a 15-min time trial, with perceived exertion measured regularly. On three of the visits, participants consumed caffeine either 35 min before steady-state exercise (PRE), at the onset of steady-state (ONS) or immediately before the time trial (DUR) phases, with a placebo consumed at the other two time points (i.e. three drinks per visit). The other visit (PLA) consisted of consuming the placebo supplement at all three time points. The placebo was taste-, colour- and calorie-matched. RESULTS: Total work performed during the time trial in PRE was 5% greater than PLA (3.53 ± 0.14 vs. 3.36 ± 0.13 kJ kg- 1 body mass; P = 0.0025), but not ONS (3.44 ± 0.13 kJ kg- 1; P = 0.3619) or DUR (3.39 ± 0.13 kJ kg- 1; P = 0.925), which were similar to PLA. Perceived exertion was lowest during steady-state exercise in the PRE condition (P
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Monteyne AJ, Coelho MOC, Porter C, Abdelrahman DR, Jameson TSO, Finnigan TJA, Stephens FB, Dirks ML, Wall BT (2020). Branched-Chain Amino Acid Fortification Does Not Restore Muscle Protein Synthesis Rates following Ingestion of Lower- Compared with Higher-Dose Mycoprotein.
J Nutr,
150(11), 2931-2941.
Abstract:
Branched-Chain Amino Acid Fortification Does Not Restore Muscle Protein Synthesis Rates following Ingestion of Lower- Compared with Higher-Dose Mycoprotein.
BACKGROUND: We have shown that ingesting a large bolus (70 g) of the fungal-derived, whole food mycoprotein robustly stimulates muscle protein synthesis (MPS) rates. OBJECTIVE: the aim of this study was to determine if a lower dose (35 g) of mycoprotein enriched with branched-chain amino acids (BCAAs) stimulates MPS to the same extent as 70 g of mycoprotein in resistance-trained young men. METHODS: Nineteen men [aged 22 ± 1 y, BMI (kg/m2): 25 ± 1] took part in a randomized, double-blind, parallel-group study. Participants received primed, continuous infusions of l-[ring-2H5]phenylalanine and ingested either 70 g mycoprotein (31.5 g protein; MYCO; n = 10) or 35 g BCAA-enriched mycoprotein (18.7 g protein: matched on BCAA content; ENR; n = 9) following a bout of unilateral resistance exercise. Blood and bilateral quadriceps muscle samples were obtained before exercise and protein ingestion and during a 4-h postprandial period to assess MPS in rested and exercised muscle. Two- and 3-factor ANOVAs were used to detect differences in plasma amino acid kinetics and mixed muscle fractional synthetic rates, respectively. RESULTS: Postprandial plasma BCAA concentrations increased more rapidly and to a larger degree in ENR compared with MYCO. MPS increased with protein ingestion (P ≤ 0.05) but to a greater extent following MYCO (from 0.025% ± 0.006% to 0.057% ± 0.004% · h-1 in rested muscle, and from 0.024% ± 0.007% to 0.072% ± 0.005% · h-1 in exercised muscle; P
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Monteyne AJ, Coelho MOC, Porter C, Abdelrahman DR, Jameson TSO, Jackman SR, Blackwell JR, Finnigan TJA, Stephens FB, Dirks ML, et al (2020). Mycoprotein ingestion stimulates protein synthesis rates to a greater extent than milk protein in rested and exercised skeletal muscle of healthy young men: a randomized controlled trial.
Am J Clin Nutr,
112(2), 318-333.
Abstract:
Mycoprotein ingestion stimulates protein synthesis rates to a greater extent than milk protein in rested and exercised skeletal muscle of healthy young men: a randomized controlled trial.
BACKGROUND: Mycoprotein is a fungal-derived sustainable protein-rich food source, and its ingestion results in systemic amino acid and leucine concentrations similar to that following milk protein ingestion. OBJECTIVE: We assessed the mixed skeletal muscle protein synthetic response to the ingestion of a single bolus of mycoprotein compared with a leucine-matched bolus of milk protein, in rested and exercised muscle of resistance-trained young men. METHODS: Twenty resistance-trained healthy young males (age: 22 ± 1 y, body mass: 82 ± 2 kg, BMI: 25 ± 1 kg·m-2) took part in a randomized, double-blind, parallel-group study. Participants received primed, continuous infusions of L-[ring-2H5]phenylalanine and ingested either 31 g (26.2 g protein: 2.5 g leucine) milk protein (MILK) or 70 g (31.5 g protein: 2.5 g leucine) mycoprotein (MYCO) following a bout of unilateral resistance-type exercise (contralateral leg acting as resting control). Blood and m. vastus lateralis muscle samples were collected before exercise and protein ingestion, and following a 4-h postprandial period to assess mixed muscle fractional protein synthetic rates (FSRs) and myocellular signaling in response to the protein beverages in resting and exercised muscle. RESULTS: Mixed muscle FSRs increased following MILK ingestion (from 0.036 ± 0.008 to 0.052 ± 0.006%·h-1 in rested, and 0.035 ± 0.008 to 0.056 ± 0.005%·h-1 in exercised muscle; P
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Coelho MOC, Monteyne AJ, Kamalanathan ID, Najdanovic-Visak V, Finnigan TJA, Stephens FB, Wall BT (2020). Short-communication: Ingestion of a nucleotide-rich mixed meal increases serum uric acid concentrations but does not affect postprandial blood glucose or serum insulin responses in young adults.
Nutrients,
12(4).
Abstract:
Short-communication: Ingestion of a nucleotide-rich mixed meal increases serum uric acid concentrations but does not affect postprandial blood glucose or serum insulin responses in young adults
Circulating uric acid concentrations have been linked to various metabolic diseases. Consumption of large boluses of nucleotides increases serum uric acid concentrations. We investigated the effect of a nucleotide-rich mixed meal on postprandial circulating uric acid, glucose, and insulin responses. Ten healthy adults participated in a randomised, controlled, double-blind, crossover trial in which they consumed a mixed-meal containing either nucleotide-depleted mycoprotein (L-NU) or high-nucleotide mycoprotein (H-NU) on two separate visits. Blood samples were collected in the postabsorptive state and throughout a 24 h postprandial period, and were used to determine circulating uric acid, glucose, and insulin concentrations. Mixed meal ingestion had divergent effects on serum uric acid concentrations across conditions (time x condition interaction; P < 0.001), with L-NU decreasing transiently (from 45 to 240 min postprandially) by ~7% (from 279 ± 16 to 257 ± 14 µmol·L−1) and H-NU resulting in a ~12% increase (from 284 ± 13 to 319 ± 12 µmol·L−1 after 210 min), remaining elevated for 12 h and returning to baseline concentrations after 24 h. There were no differences between conditions in blood glucose or serum insulin responses, nor in indices of insulin sensitivity. The ingestion of a nucleotide-rich mixed-meal increases serum uric acid concentrations for ~12 h, but does not influence postprandial blood glucose or serum insulin concentrations.
Abstract.
2019
Coelho M, Monteyne A, Dunlop M, Harris H, Morrison D, Stephens F, Wall B (2019). Mycoprotein as a possible alternative source of dietary protein to support muscle and metabolic health. Nutrition Reviews
2018
Monteyne A, Martin A, Jackson L, Corrigan N, Stringer E, Newey J, Rumbold PLS, Stevenson EJ, James LJ (2018). Whey protein consumption after resistance exercise reduces energy intake at a post-exercise meal.
European Journal of Nutrition,
57(2), 585-592.
Abstract:
Whey protein consumption after resistance exercise reduces energy intake at a post-exercise meal
Purpose: Protein consumption after resistance exercise potentiates muscle protein synthesis, but its effects on subsequent appetite in this context are unknown. This study examined appetite and energy intake following consumption of protein- and carbohydrate-containing drinks after resistance exercise. Methods: After familiarisation, 15 resistance training males (age 21 ± 1 years, body mass 78.0 ± 11.9 kg, stature 1.78 ± 0.07 m) completed two randomised, double-blind trials, consisting of lower-body resistance exercise, followed by consumption of a whey protein (PRO 23.9 ± 3.6 g protein) or dextrose (CHO 26.5 ± 3.8 g carbohydrate) drink in the 5 min post-exercise. An ad libitum meal was served 60 min later, with subjective appetite measured throughout. Drinks were flavoured and matched for energy content and volume. The PRO drink provided 0.3 g/kg body mass protein. Results: Ad libitum energy intake (PRO 3742 ± 994 kJ; CHO 4172 ± 1132 kJ; P = 0.007) and mean eating rate (PRO 339 ± 102 kJ/min; CHO 405 ± 154 kJ/min; P = 0.009) were lower during PRO. The change in eating rate was associated with the change in energy intake (R = 0.661, P = 0.007). No interaction effects were observed for subjective measures of appetite. The PRO drink was perceived as creamier and thicker, and less pleasant, sweet and refreshing (P OpenSPiltSPi 0.05). Conclusion: These results suggest whey protein consumption after resistance exercise reduces subsequent energy intake, and this might be partially mediated by a reduced eating rate. Whilst this reduced energy intake is unlikely to impair hypertrophy, it may be of value in supporting an energy deficit for weight loss.
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