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Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial

BACKGROUND: Insects have recently been identified as a more sustainable protein-dense food source and may represent a viable alternative to conventional animal-derived proteins. OBJECTIVES: We aimed to compare the impacts of ingesting lesser mealworm– and milk-derived protein on protein digestion an...

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Autores principales: Hermans, Wesley J H, Senden, Joan M, Churchward-Venne, Tyler A, Paulussen, Kevin J M, Fuchs, Cas J, Smeets, Joey S J, van Loon, Joop J A, Verdijk, Lex B, van Loon, Luc J C
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8408844/
https://www.ncbi.nlm.nih.gov/pubmed/34020450
http://dx.doi.org/10.1093/ajcn/nqab115
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author Hermans, Wesley J H
Senden, Joan M
Churchward-Venne, Tyler A
Paulussen, Kevin J M
Fuchs, Cas J
Smeets, Joey S J
van Loon, Joop J A
Verdijk, Lex B
van Loon, Luc J C
author_facet Hermans, Wesley J H
Senden, Joan M
Churchward-Venne, Tyler A
Paulussen, Kevin J M
Fuchs, Cas J
Smeets, Joey S J
van Loon, Joop J A
Verdijk, Lex B
van Loon, Luc J C
author_sort Hermans, Wesley J H
collection PubMed
description BACKGROUND: Insects have recently been identified as a more sustainable protein-dense food source and may represent a viable alternative to conventional animal-derived proteins. OBJECTIVES: We aimed to compare the impacts of ingesting lesser mealworm– and milk-derived protein on protein digestion and amino acid absorption kinetics, postprandial skeletal muscle protein synthesis rates, and the incorporation of dietary protein–derived amino acids into de novo muscle protein at rest and during recovery from exercise in vivo in humans. METHODS: In this double-blind randomized controlled trial, 24 healthy, young men ingested 30 g specifically produced, intrinsically l-[1-(13)C]-phenylalanine and l-[1-(13)C]-leucine labeled lesser mealworm– or milk-derived protein after a unilateral bout of resistance-type exercise. Primed continuous l-[ring-(2)H(5)]-phenylalanine, l-[ring-3,5-(2)H(2)]-tyrosine, and l-[1-(13)C]-leucine infusions were applied, with frequent collection of blood and muscle tissue samples. RESULTS: A total of 73% ± 7% and 77% ± 7% of the lesser mealworm and milk protein–derived phenylalanine was released into the circulation during the 5 h postprandial period, respectively, with no significant differences between groups (P < 0.05). Muscle protein synthesis rates increased after both lesser mealworm and milk protein concentrate ingestion from 0.025 ± 0.008%/h to 0.045 ± 0.017%/h and 0.028 ± 0.010%/h to 0.056 ± 0.012%/h at rest and from 0.025 ± 0.012%/h to 0.059 ± 0.015%/h and 0.026 ± 0.009%/h to 0.073 ± 0.020%/h after exercise, respectively (all P < 0.05), with no differences between groups (both P > 0.05). Incorporation of mealworm and milk protein-derived l-[1-(13)C]-phenylalanine into de novo muscle protein was greater after exercise than at rest (P < 0.05), with no differences between groups (P > 0.05). CONCLUSIONS: Ingestion of a meal-like amount of lesser mealworm–derived protein is followed by rapid protein digestion and amino acid absorption and increases muscle protein synthesis rates both at rest and during recovery from exercise. The postprandial protein handling of lesser mealworm does not differ from ingesting an equivalent amount of milk protein concentrate in vivo in humans. This trial was registered at www.trialregister.nl as NL6897.
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spelling pubmed-84088442021-09-02 Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial Hermans, Wesley J H Senden, Joan M Churchward-Venne, Tyler A Paulussen, Kevin J M Fuchs, Cas J Smeets, Joey S J van Loon, Joop J A Verdijk, Lex B van Loon, Luc J C Am J Clin Nutr Original Research Communications BACKGROUND: Insects have recently been identified as a more sustainable protein-dense food source and may represent a viable alternative to conventional animal-derived proteins. OBJECTIVES: We aimed to compare the impacts of ingesting lesser mealworm– and milk-derived protein on protein digestion and amino acid absorption kinetics, postprandial skeletal muscle protein synthesis rates, and the incorporation of dietary protein–derived amino acids into de novo muscle protein at rest and during recovery from exercise in vivo in humans. METHODS: In this double-blind randomized controlled trial, 24 healthy, young men ingested 30 g specifically produced, intrinsically l-[1-(13)C]-phenylalanine and l-[1-(13)C]-leucine labeled lesser mealworm– or milk-derived protein after a unilateral bout of resistance-type exercise. Primed continuous l-[ring-(2)H(5)]-phenylalanine, l-[ring-3,5-(2)H(2)]-tyrosine, and l-[1-(13)C]-leucine infusions were applied, with frequent collection of blood and muscle tissue samples. RESULTS: A total of 73% ± 7% and 77% ± 7% of the lesser mealworm and milk protein–derived phenylalanine was released into the circulation during the 5 h postprandial period, respectively, with no significant differences between groups (P < 0.05). Muscle protein synthesis rates increased after both lesser mealworm and milk protein concentrate ingestion from 0.025 ± 0.008%/h to 0.045 ± 0.017%/h and 0.028 ± 0.010%/h to 0.056 ± 0.012%/h at rest and from 0.025 ± 0.012%/h to 0.059 ± 0.015%/h and 0.026 ± 0.009%/h to 0.073 ± 0.020%/h after exercise, respectively (all P < 0.05), with no differences between groups (both P > 0.05). Incorporation of mealworm and milk protein-derived l-[1-(13)C]-phenylalanine into de novo muscle protein was greater after exercise than at rest (P < 0.05), with no differences between groups (P > 0.05). CONCLUSIONS: Ingestion of a meal-like amount of lesser mealworm–derived protein is followed by rapid protein digestion and amino acid absorption and increases muscle protein synthesis rates both at rest and during recovery from exercise. The postprandial protein handling of lesser mealworm does not differ from ingesting an equivalent amount of milk protein concentrate in vivo in humans. This trial was registered at www.trialregister.nl as NL6897. Oxford University Press 2021-05-21 /pmc/articles/PMC8408844/ /pubmed/34020450 http://dx.doi.org/10.1093/ajcn/nqab115 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of the American Society for Nutrition. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited
spellingShingle Original Research Communications
Hermans, Wesley J H
Senden, Joan M
Churchward-Venne, Tyler A
Paulussen, Kevin J M
Fuchs, Cas J
Smeets, Joey S J
van Loon, Joop J A
Verdijk, Lex B
van Loon, Luc J C
Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
title Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
title_full Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
title_fullStr Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
title_full_unstemmed Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
title_short Insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
title_sort insects are a viable protein source for human consumption: from insect protein digestion to postprandial muscle protein synthesis in vivo in humans: a double-blind randomized trial
topic Original Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8408844/
https://www.ncbi.nlm.nih.gov/pubmed/34020450
http://dx.doi.org/10.1093/ajcn/nqab115
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