Abstract

Plant-based proteins are considered to be less effective in their capacity to stimulate muscle protein synthesis when compared with animal-based protein sources, likely due to differences in amino acid contents. We compared the postprandial muscle protein synthetic response following the ingestion of a lysine-enriched plant-based protein product with an isonitrogenous amount of chicken. Twenty-four men (age 24 ± 5 years; BMI 22·9 ± 2·6 kg·m-2) participated in this parallel, double-blind, randomised controlled trial and consumed 40 g of protein as a lysine-enriched wheat and chickpea protein product (Plant, n 12) or chicken breast fillet (Chicken, n 12). Primed, continuous intravenous l-(ring-13C6)-phenylalanine infusions were applied while repeated blood and muscle samples were collected over a 5-h postprandial period to assess plasma amino acid responses, muscle protein synthesis rates and muscle anabolic signalling responses. Postprandial plasma leucine and essential amino acid concentrations were higher following Chicken (P < 0·001), while plasma lysine concentrations were higher throughout in Plant (P < 0·001). Total plasma amino acid concentrations did not differ between interventions (P = 0·181). Ingestion of both Plant and Chicken increased muscle protein synthesis rates from post-absorptive: 0·031 ± 0·011 and 0·031 ± 0·013 to postprandial: 0·046 ± 0·010 and 0·055 ± 0·015 % h-1, respectively (P-time < 0·001), with no differences between Plant and Chicken (time x treatment P = 0·068). Ingestion of 40 g of protein in the form of a lysine-enriched plant-based protein product increases muscle protein synthesis rates to a similar extent as an isonitrogenous amount of chicken in healthy, young men. Plant-based protein products sold as meat replacers may be as effective as animal-based protein sources to stimulate postprandial muscle protein synthesis rates in healthy, young individuals.

Highlights

  • Skeletal muscle mass maintenance is regulated by the balance between muscle protein synthesis and breakdown rates

  • Following the ingestion of the 40-g protein meal, plasma glucose concentrations (Fig. 1(a)) increased to a greater extent in plantbased meat substitute (Plant) when compared with chicken breast (Chicken)

  • Plasma insulin concentrations in Plant peaked at 38 ± 19 min, reaching concentrations of 205 ± 73 pmol l−1, and were higher when compared with Chicken, reaching peak values of 111 ± 39 pmol l−1 at 78 ± 37 min (P < 0·05)

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Summary

Introduction

Skeletal muscle mass maintenance is regulated by the balance between muscle protein synthesis and breakdown rates. To compensate for the proposed lesser anabolic potential of plant-based proteins, more of the plant-based protein could be consumed to induce a similar postprandial increase in muscle protein synthesis rates when compared with a high-quality animal-based protein source[6]. We aimed to compare the muscle protein synthetic response following the ingestion of an ample amount of a plant-based, whole-food protein source (a meat alternative) with an equivalent amount of an animal-based protein source. We hypothesised that the postprandial muscle protein synthetic response following the ingestion of an ample amount of such a plant-based meat alternative would not differ from the ingestion of an isonitrogenous amount of chicken. We assessed basal and postprandial muscle protein synthesis rates using contemporary stable isotope methodology following ingestion of 40 g of protein provided via a lysine-enriched, wheat and chickpea protein-based product or an isonitrogenous amount of chicken in twenty-four healthy, young men

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