Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2018 Dec;50(12):1685-1695.
doi: 10.1007/s00726-018-2640-5. Epub 2018 Aug 30.

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

Stefan H M Gorissen  1 , Julie J R Crombag  1 , Joan M G Senden  1 , W A Huub Waterval  2 , Jörgen Bierau  2 , Lex B Verdijk  1 , Luc J C van Loon  3
Affiliations

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

Stefan H M Gorissen et al. Amino Acids. 2018 Dec.

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.

Keywords: Essential amino acid; Leucine; Muscle protein synthesis; Plant-based protein; Protein blend.

PubMed Disclaimer

Conflict of interest statement

Conflict of interest

SHMG, JJRC, JMGS, WAHW, and JB reported no conflicts of interest. LJCvL and LBV have received speaking honoraria or consulting fees from Friesland Campina and Nutricia Research. The industrial partners have contributed to the project through regular discussions.

Ethical approval

All procedures performed in studies involving human participants were in accordance with the ethical standards of the institutional and/or national research committee and with the 1964 Helsinki declaration and its later amendments or comparable ethical standards. This article does not contain any studies with animals performed by any of the authors.

Figures

Fig. 1
Fig. 1
Mean (± SEM) protein content (% of raw material) of various dietary protein sources and human skeletal muscle tissue based on the determined nitrogen content multiplied by 6.25 as the standard conversion factor. White bars represent plant-based protein sources, grey bars represent animal-derived protein sources, and black bar represents human skeletal muscle protein
Fig. 2
Fig. 2
Mean (± SEM) essential amino acid (EAA) contents (% 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 black bar represents human skeletal muscle protein. Dashed line represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007). Note: EAA is the sum of His, Ile, Leu, Lys, Met, Phe, Thr, and Val. Trp was not measured
Fig. 3
Fig. 3
Mean (± SEM) leucine (a), isoleucine (b), and valine (c) contents (% 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 black bar represents human muscle. Dashed line represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007)
Fig. 4
Fig. 4
Mean (± SEM) lysine (a), methionine (b), histidine (c), phenylalanine (d), and threonine (e) contents (% 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 black bar represents human muscle. Dashed line represents the amino acid requirements for adults (WHO/FAO/UNU Expert Consultation 2007)
See this image and copyright information in PMC

References

    1. Atherton PJ, Smith K, Etheridge T, Rankin D, Rennie MJ. Distinct anabolic signalling responses to amino acids in C2C12 skeletal muscle cells. Amino Acids. 2010;38(5):1533–1539. doi: 10.1007/s00726-009-0377-x. - DOI - PubMed
    1. Beals JW, Sukiennik RA, Nallabelli J, Emmons RS, van Vliet S, Young JR, Ulanov AV, Li Z, Paluska SA, De Lisio M, Burd NA. Anabolic sensitivity of postprandial muscle protein synthesis to the ingestion of a protein-dense food is reduced in overweight and obese young adults. Am J Clin Nutr. 2016;104(4):1014–1022. doi: 10.3945/ajcn.116.130385. - DOI - PubMed
    1. Bleakley S, Hayes M. Algal proteins: extraction, application, and challenges concerning production. Foods. 2017;6(5):33. doi: 10.3390/foods6050033. - DOI - PMC - PubMed
    1. Borack MS, Reidy PT, Husaini SH, Markofski MM, Deer RR, Richison AB, Lambert BS, Cope MB, Mukherjea R, Jennings K, Volpi E, Rasmussen BB. Soy-dairy protein blend or whey protein isolate ingestion induces similar postexercise muscle mechanistic target of rapamycin complex 1 signaling and protein synthesis responses in older men. J Nutr. 2016;146(12):2468–2475. doi: 10.3945/jn.116.231159. - DOI - PMC - PubMed
    1. Brown EC, DiSilvestro RA, Babaknia A, Devor ST. Soy versus whey protein bars: effects on exercise training impact on lean body mass and antioxidant status. Nutr J. 2004;3:22. doi: 10.1186/1475-2891-3-22. - DOI - PMC - PubMed