High moisture extrusion of a dietary protein blend impairs in vitro digestion and delays in vivo postprandial plasma amino acid availability in humans.

BACKGROUND: Industrial processing can alter the structural complexity of dietary proteins and, potentially, their digestion and absorption upon ingestion. High moisture extrusion (HME), a common processing method used to produce meat alternative products, affects in vitro digestion, but human data are lacking. We hypothesised that HME of a mycoprotein/pea protein blend would impair in vitro digestion and in vivo postprandial plasma amino acid availability. METHODS: In Study A nine healthy volunteers completed two experimental trials in a randomised, double-blind, cross-over design. Participants consumed a beverage containing 25 g protein from a 'dry' blend (CON) of mycoprotein/pea protein (39/61%) or a HME content matched blend (EXT). Arterialised-venous blood samples were collected in the postabsorptive state and regularly over a 5 h postprandial period to assess plasma amino acid concentrations. In Study B, in vitro digestibility of the two beverages were assessed using BCA assay and optical-fluorescence microscopy at baseline, during and following gastric and intestinal digestion using the INFOGEST model of digestion. RESULTS: Protein ingestion increased plasma total, essential (EAA), and branched-chain amino acid (BCAA) concentrations (time effect; P<0.0001), but more rapidly and to a greater magnitude in the CON compared with the EXT condition (condition x time interaction; P<0.0001). This resulted in greater plasma availability of EAA and BCAA concentrations during the early postprandial period (0-150 min). These data were corroborated by the in vitro approach which showed greater protein availability in the CON (2150 ± 129 mg·mL-1) compared with EXT (590 ± 41 mg·mL-1) during the gastric phase. Fluorescence microscopy revealed clear structural differences between the two conditions. CONCLUSIONS: These data demonstrate that HME delays in vivo plasma amino acid availability following ingestion of a mycoprotein/pea protein blend. This is likely due to impaired gastric phase digestion as a result of HME induced aggregate formation in the pea protein. CLINICAL TRIALS: NCT05584358.

A ketone monoester drink reduces postprandial blood glucose concentrations in adults with type 2 diabetes: a randomised controlled trial.

AIMS/HYPOTHESIS: The aim of the present study was to conduct a randomised, placebo-controlled, double-blind, crossover trial to determine whether pre-meal ketone monoester ingestion reduces postprandial glucose concentrations in individuals with type 2 diabetes. METHODS: In this double-blind, placebo-controlled, crossover design study, ten participants with type 2 diabetes (age 59±1.7 years, 50% female, BMI 32±1 kg/m2, HbA1c 54±2 mmol/mol [7.1±0.2%]) were randomised using computer-generated random numbers. The study took place at the Nutritional Physiology Research Unit, University of Exeter, Exeter, UK. Using a dual-glucose tracer approach, we assessed glucose kinetics after the ingestion of a 0.5 g/kg body mass ketone monoester (KME) or a taste-matched non-caloric placebo before a mixed-meal tolerance test. The primary outcome measure was endogenous glucose production. Secondary outcome measures were total glucose appearance rate and exogenous glucose appearance rate, glucose disappearance rate, blood glucose, serum insulin, ß-OHB and NEFA levels, and energy expenditure. RESULTS: Data for all ten participants were analysed. KME ingestion increased mean ± SEM plasma beta-hydroxybutyrate from 0.3±0.03 mmol/l to a peak of 4.3±1.2 mmol/l while reducing 2 h postprandial glucose concentrations by ~18% and 4 h postprandial glucose concentrations by ~12%, predominately as a result of a 28% decrease in the 2 h rate of glucose appearance following meal ingestion (all p<0.05). The reduction in blood glucose concentrations was associated with suppressed plasma NEFA concentrations after KME ingestion, with no difference in plasma insulin concentrations between the control and KME conditions. Postprandial endogenous glucose production was unaffected by KME ingestion (mean ± SEM 0.76±0.15 and 0.88±0.10 mg kg-1 min-1 for the control and KME, respectively). No adverse effects of KME ingestion were observed. CONCLUSIONS/INTERPRETATION: KME ingestion appears to delay glucose absorption in adults with type 2 diabetes, thereby reducing postprandial glucose concentrations. Future work to explore the therapeutic potential of KME supplementation in type 2 diabetes is warranted. TRIAL REGISTRATION: ClinicalTrials.gov NCT05518448. FUNDING: This project was supported by a Canadian Institutes of Health Research (CIHR) Project Grant (PJT-169116) and a Natural Sciences and Engineering Research Council (NSERC) Discovery Grant (RGPIN-2019-05204) awarded to JPL and an Exeter-UBCO Sports Health Science Fund Project Grant awarded to FBS and JPL.

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).

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.

Carbohydrate and Protein Co-Ingestion Postexercise Does Not Improve Next-Day Performance in Trained Cyclists.

Supplementing postexercise carbohydrate (CHO) intake with protein has been suggested to enhance recovery from endurance exercise. The aim of this study was to investigate whether adding protein to the recovery drink can improve 24-hr recovery when CHO intake is suboptimal. In a double-blind crossover design, 12 trained men performed three 2-day trials consisting of constant-load exercise to reduce glycogen on Day 1, followed by ingestion of a CHO drink (1.2 g·kg-1·2 hr-1) either without or with added whey protein concentrate (CHO + PRO) or whey protein hydrolysate (CHO + PROH) (0.3 g·kg-1·2 hr-1). Arterialized blood glucose and insulin responses were analyzed for 2 hr postingestion. Time-trial performance was measured the next day after another bout of glycogen-reducing exercise. The 30-min time-trial performance did not differ between the three trials (M ± SD, 401 ± 75, 411 ± 80, 404 ± 58 kJ in CHO, CHO + PRO, and CHO + PROH, respectively, p = .83). No significant differences were found in glucose disposal (area under the curve [AUC]) between the postexercise conditions (364 ± 107, 341 ± 76, and 330 ± 147, mmol·L-1·2 hr-1, respectively). Insulin AUC was lower in CHO (18.1 ± 7.7 nmol·L-1·2 hr-1) compared with CHO + PRO and CHO + PROH (24.6 ± 12.4 vs. 24.5 ± 10.6, p = .036 and .015). No difference in insulin AUC was found between CHO + PRO and CHO + PROH. Despite a higher acute insulin response, adding protein to a CHO-based recovery drink after a prolonged, high-intensity exercise bout did not change next-day exercise capacity when overall 24-hr macronutrient and caloric intake was controlled.