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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. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

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 < 0.0001) compared with ENR (from 0.031% ± 0.003% to 0.043% ± 0.005% · h-1 in rested muscle, and 0.027% ± 0.005% to 0.052% ± 0.005% · h-1 in exercised muscle; P < 0.01) ingestion. Postprandial MPS rates were greater in MYCO compared with ENR (P < 0.01).Conclusions: The ingestion of lower-dose BCAA-enriched mycoprotein stimulates resting and postexercise MPS rates, but to a lesser extent compared with the ingestion of a BCAA-matched 70-g mycoprotein bolus in healthy young men. This trial was registered at clinicaltrials.gov as 660065600. [ABSTRACT FROM AUTHOR]

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  <0.01) but to a greater extent following MYCO ingestion (from 0.025 ± 0.006 to 0.057 ± 0.004%·h−1 in rested, and 0.024 ± 0.007 to 0.072 ± 0.005%·h−1 in exercised muscle; P  <0.0001) (treatment × time interaction effect; P  <0.05). Postprandial FSRs trended to be greater in MYCO compared with MILK (0.065 ± 0.004 compared with 0.054 ± 0.004%·h−1, respectively; P  = 0.093) and the postprandial rise in FSRs was greater in MYCO compared with MILK (Delta 0.040 ± 0.006 compared with Delta 0.018 ± 0.005%·h−1, respectively; P  <0.01). Conclusions The ingestion of a single bolus of mycoprotein stimulates resting and postexercise muscle protein synthesis rates, and to a greater extent than a leucine-matched bolus of milk protein, in resistance-trained young men. This trial was registered at clinicaltrials.gov as 660065600. [ABSTRACT FROM AUTHOR]

The world's population is expanding, leading to an increased global requirement for dietary protein to support health and adaptation in various populations. Though a strong evidence base supports the nutritional value of animal-derived dietary proteins, mounting challenges associated with sustainability of these proteins have led to calls for the investigation of alternative, non–animal-derived dietary protein sources. Mycoprotein is a sustainably produced, protein-rich, high-fiber, whole food source derived from the fermentation of fungus. Initial investigations in humans demonstrated that mycoprotein consumption can lower circulating cholesterol concentrations. Recent data also report improved acute postprandial glycemic control and a potent satiety effect following mycoprotein ingestion. It is possible that these beneficial effects are attributable to the amount and type of dietary fiber present in mycoprotein. Emerging data suggest that the amino acid composition and bioavailability of mycoprotein may also position it as a promising dietary protein source to support skeletal muscle protein metabolism. Mycoprotein may be a viable dietary protein source to promote training adaptations in athletes and the maintenance of muscle mass to support healthy aging. Herein, current evidence underlying the metabolic effects of mycoprotein is reviewed, and the key questions to be addressed are highlighted. [ABSTRACT FROM AUTHOR]