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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 it...

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Autores principales: West, Sam, Monteyne, Alistair J., Whelehan, Gráinne, van der Heijden, Ino, Abdelrahman, Doaa R., Murton, Andrew J., Finnigan, Tim J. A., Stephens, Francis B., Wall, Benjamin T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Physiological Society 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10655824/
https://www.ncbi.nlm.nih.gov/pubmed/37529834
http://dx.doi.org/10.1152/ajpendo.00166.2023
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author West, Sam
Monteyne, Alistair J.
Whelehan, Gráinne
van der Heijden, Ino
Abdelrahman, Doaa R.
Murton, Andrew J.
Finnigan, Tim J. A.
Stephens, Francis B.
Wall, Benjamin T.
author_facet West, Sam
Monteyne, Alistair J.
Whelehan, Gráinne
van der Heijden, Ino
Abdelrahman, Doaa R.
Murton, Andrew J.
Finnigan, Tim J. A.
Stephens, Francis B.
Wall, Benjamin T.
author_sort West, Sam
collection PubMed
description 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).
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spelling pubmed-106558242023-08-02 Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals West, Sam Monteyne, Alistair J. Whelehan, Gráinne van der Heijden, Ino Abdelrahman, Doaa R. Murton, Andrew J. Finnigan, Tim J. A. Stephens, Francis B. Wall, Benjamin T. Am J Physiol Endocrinol Metab Research Article 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). American Physiological Society 2023-09-01 2023-08-02 /pmc/articles/PMC10655824/ /pubmed/37529834 http://dx.doi.org/10.1152/ajpendo.00166.2023 Text en Copyright © 2023 The Authors. https://creativecommons.org/licenses/by/4.0/Licensed under Creative Commons Attribution CC-BY 4.0 (https://creativecommons.org/licenses/by/4.0/) . Published by the American Physiological Society.
spellingShingle Research Article
West, Sam
Monteyne, Alistair J.
Whelehan, Gráinne
van der Heijden, Ino
Abdelrahman, Doaa R.
Murton, Andrew J.
Finnigan, Tim J. A.
Stephens, Francis B.
Wall, Benjamin T.
Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
title Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
title_full Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
title_fullStr Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
title_full_unstemmed Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
title_short Ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
title_sort ingestion of mycoprotein, pea protein, and their blend support comparable postexercise myofibrillar protein synthesis rates in resistance-trained individuals
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10655824/
https://www.ncbi.nlm.nih.gov/pubmed/37529834
http://dx.doi.org/10.1152/ajpendo.00166.2023
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