Cited by 170Muscle metabolism and nutritionProteins in Food SystemsMuscle Physiology and Disorders

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The Anabolic Response to Plant-Based Protein Ingestion

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Pinckaers, Philippe J. M., Trommelen, Jorn, Snijders, Tim, van Loon, Luc J. C.·2021·Sports Medicine

Abstract

There is a global trend of an increased interest in plant-based diets. This includes an increase in the consumption of plant-based proteins at the expense of animal-based proteins. Plant-derived proteins are now also frequently applied in sports nutrition. So far, we have learned that the ingestion of plant-derived proteins, such as soy and wheat protein, result in lower post-prandial muscle protein synthesis responses when compared with the ingestion of an equivalent amount of animal-based protein. The lesser anabolic properties of plant-based versus animal-derived proteins may be attributed to differences in their protein digestion and amino acid absorption kinetics, as well as to differences in amino acid composition between these protein sources. Most plant-based proteins have a low essential amino acid content and are often deficient in one or more specific amino acids, such as lysine and methionine. However, there are large differences in amino acid composition between various plant-derived proteins or plant-based protein sources. So far, only a few studies have directly compared the muscle protein synthetic response following the ingestion of a plant-derived protein versus a high(er) quality animal-derived protein. The proposed lower anabolic properties of plant- versus animal-derived proteins may be compensated for by (i) consuming a greater amount of the plant-derived protein or plant-based protein source to compensate for the lesser quality; (ii) using specific blends of plant-based proteins to create a more balanced amino acid profile; (iii) fortifying the plant-based protein (source) with the specific free amino acid(s) that is (are) deficient. Clinical studies are warranted to assess the anabolic properties of the various plant-derived proteins and their protein sources in vivo in humans and to identify the factors that may or may not compromise the capacity to stimulate post-prandial muscle protein synthesis rates. Such work is needed to determine whether the transition towards a more plant-based diet is accompanied by a transition towards greater dietary protein intake requirements.

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Crossref · 10.1007/s40279-021-01540-8

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Figures

Fig. 1 Essential amino acid (EAA, Panel a), leucine (Panel b), lysine (Panel c), and methionine (Panel d) contents (expressed as % of total protein) of various dietary protein sources and human skeletal muscle protein. White bars represent plant-based protein sources, grey bars represent animal-derived protein sources, and the black bar represents human skeletal muscle protein. Dashed line represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007 [58]). Note: EAA is the sum of histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, and valine, as tryptophan was not measured. Values obtained from multiple products are expressed as mean (± SEM). This figure represents an extension from data previously presented by Gorissen et al. 2018 [39], assessed using the same method. 1 Flour, 2 Protein concentrate/isolate, 3 Freeze-dried raw product
Fig. 1 Essential amino acid (EAA, Panel a), leucine (Panel b), lysine (Panel c), and methionine (Panel d) contents (expressed as % of total protein) of various dietary protein sources and human skeletal muscle protein. White bars represent plant-based protein sources, grey bars represent animal-derived protein sources, and the black bar represents human skeletal muscle protein. Dashed line represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007 [58]). Note: EAA is the sum of histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, and valine, as tryptophan was not measured. Values obtained from multiple products are expressed as mean (± SEM). This figure represents an extension from data previously presented by Gorissen et al. 2018 [39], assessed using the same method. 1 Flour, 2 Protein concentrate/isolate, 3 Freeze-dried raw productCC BY · PubMed Central
Fig. 2 Categorical representation of the feasibility of consuming 20 g protein provided by ingesting the whole food source (x-axis), with the amount of food that needs to be consumed expressed as servings with the concomitant energy intake equivalent (y-axis). Serving sizes: meat/salmon: ~ 100 g, egg: ~ 120 g (2 eggs), soy: ~ 100 g, pea: ~ 150 g, chickpea: ~ 150 g, peanut: ~ 50 g, bread (wheat): ~ 70 g (2 slices), milk: ~ 200 mL, corn: ~ 150 g, oats ~ 40 g (raw), quinoa: ~ 75 g (raw), brown rice: ~ 75 g (raw), potato: 175 g
Fig. 2 Categorical representation of the feasibility of consuming 20 g protein provided by ingesting the whole food source (x-axis), with the amount of food that needs to be consumed expressed as servings with the concomitant energy intake equivalent (y-axis). Serving sizes: meat/salmon: ~ 100 g, egg: ~ 120 g (2 eggs), soy: ~ 100 g, pea: ~ 150 g, chickpea: ~ 150 g, peanut: ~ 50 g, bread (wheat): ~ 70 g (2 slices), milk: ~ 200 mL, corn: ~ 150 g, oats ~ 40 g (raw), quinoa: ~ 75 g (raw), brown rice: ~ 75 g (raw), potato: 175 gCC BY · PubMed Central
Fig. 3 Overview of potential issues and solutions to optimise the anabolic response following plant-based protein consumption. (1) For plant-based foods with a high protein quality, but low protein content (e.g. potato), extraction of high-quality protein isolates forms an effective method to allow ingestion of a desired amount of protein. (2) For plant-based food sources with deficiencies in specific amino acids (e.g. corn: low in lysine), a protein isolate or concentrate can be fortified with the deficient free amino acid(s) to improve the amino acid content profile. (3) Plant-based food sources with deficiencies in specific essential amino acids can be combined to improve the overall amino acid profile of the protein blend. For example, peas are low in methionine but high in lysine; in contrast, brown rice is high in methionine but low in lysine. A blend combining pea and brown rice would meet overall amino acid requirements. (4) When plant-based food sources (or protein isolates) are deficient in one or more amino acids (e.g. lentils, wheat), this may be compensated for by simply ingesting a greater amount of the plant-based protein source. Illustrations: the scale balance represents the amount of food to be consumed to provide 20 g protein, unless otherwise indicated. Weight for brown rice and lentils represent cooked amounts. Dashed horizontal line in graphs represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007 [58]). EAA Essential amino acid
Fig. 3 Overview of potential issues and solutions to optimise the anabolic response following plant-based protein consumption. (1) For plant-based foods with a high protein quality, but low protein content (e.g. potato), extraction of high-quality protein isolates forms an effective method to allow ingestion of a desired amount of protein. (2) For plant-based food sources with deficiencies in specific amino acids (e.g. corn: low in lysine), a protein isolate or concentrate can be fortified with the deficient free amino acid(s) to improve the amino acid content profile. (3) Plant-based food sources with deficiencies in specific essential amino acids can be combined to improve the overall amino acid profile of the protein blend. For example, peas are low in methionine but high in lysine; in contrast, brown rice is high in methionine but low in lysine. A blend combining pea and brown rice would meet overall amino acid requirements. (4) When plant-based food sources (or protein isolates) are deficient in one or more amino acids (e.g. lentils, wheat), this may be compensated for by simply ingesting a greater amount of the plant-based protein source. Illustrations: the scale balance represents the amount of food to be consumed to provide 20 g protein, unless otherwise indicated. Weight for brown rice and lentils represent cooked amounts. Dashed horizontal line in graphs represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007 [58]). EAA Essential amino acidCC BY · PubMed Central
Fig. 4 Amount of the selected whole-food protein sources to be consumed to allow ingestion of 20 g protein. Illustrated are meat, soy, pea, chickpea, brown rice and potato in order of protein content (from high to low)
Fig. 4 Amount of the selected whole-food protein sources to be consumed to allow ingestion of 20 g protein. Illustrated are meat, soy, pea, chickpea, brown rice and potato in order of protein content (from high to low)CC BY · PubMed Central

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Metadata

Authors
Pinckaers, P. J. M., Trommelen, J., Snijders, T., & van Loon, L. J. C.
Affiliations
Maastricht University Medical Centre (NL)
Venue
Sports Medicine
Published
2021-09
Volume
51
Issue
S1
Pages
59-74
ISSN
  • 0112-1642 (ISSN-L)
  • 1179-2035
OpenAlex
W3200956314
Cited by
170
References
131
Citations by year
2026: 38 · 2025: 44 · 2024: 37 · 2023: 23 · 2022: 22 · 2021: 6
FWCI
2.78
Type
journal article
Language
en
Open access
Locations
  • Sports Medicine (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research Publications (Maastricht University) (publishedVersion, cc-by)
  • VUBIR (Vrije Universiteit Brussel) (submittedVersion)
  • Research Publications (Maastricht University) (submittedVersion, cc-by)
Funders
Gran Sasso Science Institute
Topics
  • Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords
plant proteins, muscle protein synthesis, anabolic response, soy protein, wheat proteins, amino acid composition, essential amino acids, lysine, methionine, protein digestion, sports nutrition, protein requirements, plant-based diet
MeSH terms
Amino Acids, Essential, Animals, Dietary Proteins, Eating, Humans, Muscle Proteins, Muscle, Skeletal

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