Protein content and amino acid composition of commercially available plant-based protein isolates

Gorissen, Stefan H. M.; Crombag, Julie J. R.; Senden, Joan M. G.; Waterval, W. A. Huub; Bierau, Jörgen; Verdijk, Lex B.; van Loon, Luc J. C.

doi:10.1007/s00726-018-2640-5

Cited by 1,169Muscle metabolism and nutritionFood and Agricultural SciencesProteins in Food Systems

Protein content and amino acid composition of commercially available plant-based protein isolates

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Gorissen, Stefan H. M., Crombag, Julie J. R., Senden, Joan M. G., Waterval, W. A. Huub, Bierau, Jörgen, Verdijk, Lex B., van Loon, Luc J. C.·2018·Amino Acids

DOI 10.1007/s00726-018-2640-5PMC PMC6245118

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Abstract

The postprandial rise in essential amino acid (EAA) concentrations modulates the increase in muscle protein synthesis rates after protein ingestion. The EAA content and AA composition of the dietary protein source contribute to the differential muscle protein synthetic response to the ingestion of different proteins. Lower EAA contents and specific lack of sufficient leucine, lysine, and/or methionine may be responsible for the lower anabolic capacity of plant-based compared with animal-based proteins. We compared EAA contents and AA composition of a large selection of plant-based protein sources with animal-based proteins and human skeletal muscle protein. AA composition of oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, potato, milk, whey, caseinate, casein, egg, and human skeletal muscle protein were assessed using UPLC-MS/MS. EAA contents of plant-based protein isolates such as oat (21%), lupin (21%), and wheat (22%) were lower than animal-based proteins (whey 43%, milk 39%, casein 34%, and egg 32%) and muscle protein (38%). AA profiles largely differed among plant-based proteins with leucine contents ranging from 5.1% for hemp to 13.5% for corn protein, compared to 9.0% for milk, 7.0% for egg, and 7.6% for muscle protein. Methionine and lysine were typically lower in plant-based proteins (1.0 ± 0.3 and 3.6 ± 0.6%) compared with animal-based proteins (2.5 ± 0.1 and 7.0 ± 0.6%) and muscle protein (2.0 and 7.8%, respectively). In conclusion, there are large differences in EAA contents and AA composition between various plant-based protein isolates. Combinations of various plant-based protein isolates or blends of animal and plant-based proteins can provide protein characteristics that closely reflect the typical characteristics of animal-based proteins.

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Animal protein generally contains higher essential amino acid content than plant protein.
“Animal protein generally contains higher EAA content than plant protein [61]”
From Animal Protein versus Plant Protein in Supporting Lean Mass and Muscle Strength: A Systematic Review and Meta-Analysis of Randomized Controlled Trials (2021) · cites this paper as [61]
Proteins contain abundant hydrophobic groups and most gelation processes involve protein unfolding exposing additional hydrophobic residues, which can make hydrophobic interaction a major driving force in gel network formation.
“In details, proteins contain abundant hydrophobic groups and most gelation processes involve protein unfolding exposing additional hydrophobic residues (X. Wei, Monahan, et al. 2023; Gorissen et al. 2018), which can make hydrophobic interaction a major driving force in gel network formation.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Gorissen et al. 2018
The Methods section describes hydrolysis for amino acid analysis, and the Results section reports amino acid profiles; neither addresses protein gelation. Searches for hydrophobic groups, unfolding, and gel-network formation found no passage in our copy supporting the attributed mechanism. The indexed passages provide no page numbers. (LLM, conf=0.75)
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Differences in protein absorbability are ameliorated after protein purification through removal of nonprotein constituents to produce protein isolates.
“However, differences in protein absorbability are ameliorated after protein purification through removal of nonprotein constituents to produce protein isolates [[80], [81], [82]].”
From Nutritional Considerations for the Vegan Athlete (2023) · cites this paper as [80]
Plant proteins are often low in leucine, and additional leucine might potentiate their postprandial anabolic response.
“Plant proteins are often low in leucine [80], and it is thought that additional leucine might potentiate their postprandial anabolic response.”
From Nutritional Considerations for the Vegan Athlete (2023) · cites this paper as [80]

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Background
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Authors: Gorissen, S. H. M., Crombag, J. J. R., Senden, J. M. G., Waterval, W. A. H., Bierau, J., Verdijk, L. B., & van Loon, L. J. C.
Affiliations: Maastricht University Medical Centre (NL)
ORCID: Gorissen, Stefan H. M.
Senden, Joan M. G.
Bierau, Jörgen
Verdijk, Lex B.
Venue: Amino Acids
Publisher: Springer Science and Business Media LLC
Published: 2018-08-30
Volume: 50
Issue: 12
Pages: 1685-1695
ISSN: 0939-4451 (ISSN-L)
1438-2199
DOI: 10.1007/s00726-018-2640-5
PMC: PMC6245118
OpenAlex: W2889500241
Cited by: 1,169
References: 52
Citations by year: 2026: 196 · 2025: 218 · 2024: 214 · 2023: 172 · 2022: 141 · 2021: 121 · 2020: 83 · 2019: 20 · 2018: 2
FWCI: 31.29
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0 (tdm)
Locations: Amino Acids (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, other-oa)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Research Publications (Maastricht University) (publishedVersion, cc-by)
Research Bank (Australian Catholic University) (submittedVersion)
VUBIR (Vrije Universiteit Brussel) (submittedVersion)
Research Publications (Maastricht University) (submittedVersion, other-oa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Keywords: amino acid composition, essential amino acids, leucine, methionine, lysine, muscle protein synthesis, whey protein, casein, egg proteins, oat protein, lupin protein, wheat proteins, hemp protein, microalgal proteins, pea protein, corn protein, potato protein, milk protein, protein blends
MeSH terms: Amino Acids, Amino Acids, Essential, Chromatography, Liquid, Humans, Muscle Proteins, Protein Biosynthesis, Plant Proteins, Dietary, Muscle, Skeletal, Tandem Mass Spectrometry, Functional Food

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Protein content and amino acid composition of commercially available plant-based protein isolates

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