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

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

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.

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)

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