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Purpose: Whey protein ingestion is typically considered an optimal dietary strategy tomaximizemyofibrillar protein synthesis (MyoPS) after resistance exercise. Although single-source plant protein ingestion is typically less effective, at least partly, due to less favorable amino acid profiles, this could theoretically be overcome by blending plant-based proteins with complementary amino acid profiles. We compared the postexercise MyoPS response after the ingestion of a novel plant-derived protein blend with an isonitrogenous bolus of whey protein. Methods: Ten healthy, resistance-trained, young adults (male/female: 8/2; age: 26 ± 6 yr; BMI: 24 ± 3 kg·m-2) received a primed continuous infusion of L-[ring-²H5]-phenylalanine and completed a bout of bilateral leg resistance exercise before ingesting 32 g protein from whey (WHEY) or a plant protein blend (BLEND; 39.5% pea, 39.5% brown rice, 21.0% canola) in a randomized, double-blind crossover fashion. Blood and muscle samples were collected at rest, and 2 and 4 h after exercise and protein ingestion, to assess plasma amino acid concentrations, and postabsorptive and postexercise MyoPS rates. Results: Plasma essential amino acid availability over the 4 h postprandial postexercise period was ~44% higher inWHEY compared with BLEND (P = 0.04). From equivalent postabsorptive values (WHEY, 0.042 ± 0.020%·h-1; BLEND, 0.043 ± 0.015%·h-1) MyoPS rates increased after exercise and protein ingestion (time effect; P < 0.001) over a 0- to 2-h period (WHEY, 0.085 ± 0.037%·h-1; BLEND, 0.080 ± 0.037%·h-1) and 2- to 4-h period (WHEY, 0.085 ± 0.036%·h-1; BLEND, 0.086 ± 0.034%·h-1), with no differences between conditions during either period or throughout the entire (0-4 h) postprandial period (time-condition interactions; all P > 0.05). Conclusions: Ingestion of a novel plant-based protein blend stimulates postexercise MyoPS to an equivalent extent as whey protein, demonstrating the utility of plant protein blends to optimize postexercise skeletal muscle reconditioning. [ABSTRACT FROM AUTHOR]

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]

We characterized daily dietary protein intakes, focusing on protein source (animal and nonanimal) and form (whole-foods and supplemental) in young (18-40 years) resistance trained (training ≥ 3×/week for ≥ 6 months; TRA; male, n = 30; female, n = 14) and recreationally active (no structured training; REC; male, n = 30; female, n = 30) individuals. Using 3-day weighed food diaries from 10 previous studies, we assessed macronutrient intakes using dietary analysis software. Energy intakes trended greater in TRA compared with REC (p = .056) and were greater in males than females (p = .006). TRA consumed greater (p = .002) proportions of daily energy intake as protein than REC (23 ± 6 vs. 19 ± 5%Energy), which also trended greater in males compared with females (22 ± 3 vs. 20 ± 2%Energy; p = .060). Absolute (p < .001) and relative (to body mass [BM]; p < .001) protein intakes were greater in TRA (males, 159 ± 54 g/day or 1.6 ± 0.7 g·kg-1 BM·day-1; females, 105 ± 40 g/day or 2.0 ± 0.6 g·kg-1 BM·day-1; p < .001) than REC (males, 103 ± 37 g/day or 1.3 ± 0.5 g·kg-1 BM·day-1; females, 85 ± 23 g/day or 1.3 ± 0.4 g·kg-1 BM·day-1; p < .001), with absolute (p = .025), but not relative (p = .129) intakes greater in males. A greater proportion of total protein was consumed from animal compared with nonanimal in TRA (68% vs. 32%, respectively; p < .001) and REC (64% vs. 36%, respectively; p < .001); the skew driven exclusively by males (72% vs. 28%, respectively; p < .001). A greater proportion (∼92%) of total protein was consumed as whole-foods compared with supplemental, irrespective of training status or sex (p < .001). We show animal and whole-food-derived proteins contribute the majority to daily dietary protein intakes in TRA and REC young males and females.

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 - 2 H 5 ]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).