Protein digestibility-corrected amino acid scores (PDCAAS) for soy protein isolates and concentrate: Criteria for evaluation

Hughes, Glenna J.; Ryan, David J.; Mukherjea, Ratna; Schasteen, Charles S.

doi:10.1021/jf203220v

Cited by 316Food and Agricultural SciencesProteins in Food SystemsMuscle metabolism and nutrition

Protein digestibility-corrected amino acid scores (PDCAAS) for soy protein isolates and concentrate: Criteria for evaluation

Hughes, Glenna J., Ryan, David J., Mukherjea, Ratna, Schasteen, Charles S.·2011·Journal of Agricultural and Food Chemistry

DOI 10.1021/jf203220v

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Abstract

Protein quality, as determined by the PDCAAS method, is a measure of a protein's ability to provide adequate levels of essential amino acids for human needs. PDCAAS is calculated using an amino acid profile and true digestibility of a food protein. Soy protein is recognized as a high quality plant protein, but published PDCAAS values may vary based on the soy protein ingredient as well as the reproducibility and accuracy of the testing methods. Comparison of PDCAAS values for four differently processed soy ingredients, including three isolated soy proteins (ISP) and one soy protein concentrate (SPC), was made using two different laboratories with evaluation of the impact of the reproducibility and accuracy of amino acid profiles. PDCAAS calculations, using amino acid values from one laboratory, yielded a truncated PDCAAS of 1.00 for all four ingredients, while a second laboratory provided statistically significantly lower scores (0.95-1.00). We conclude that analytical method error can be a significant contributor to PDCAAS differences and can be mitigated by the application of amino acid nitrogen recovery correction factors.

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The protein digestibility of soy protein isolate is 96% or higher, while the protein digestibility of soy flour is only 84%.
“the protein digestibility of soy protein isolate is 96% or higher, while the protein digestibility of soy flour is only 84% [24,25].”
From Plant Proteins: Assessing Their Nutritional Quality and Effects on Health and Physical Function (2020) · cites this paper as [25]

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Background
Effects of rice bran content on plant-based simulated meat: From the aspects of apparent properties and structural characteristics
Jiang, R., Xiao, Z., Huo, J., Wang, H., Li, H., Su, S., Duan, Y., & Gao, Y. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.131842 · Cited by 50 · see citing works
Effect of Fractionation and Processing Conditions on the Digestibility of Plant Proteins as Food Ingredients
del Rio, A. R., Boom, R. M., & Janssen, A. E. M. (2022) · Foods · doi:10.3390/foods11060870 · Cited by 51 · see citing works
“Commercial PC and PI have been used in in vivo rat assays, showing a small variation in PDCAAS, the true or standard ileal digestibility, of soybean ingredients [31,32].”
Method
Breeding Canola (Brassica napus L.) for Protein in Feed and Food
So, K. K. Y., & Duncan, R. (2021) · Plants · doi:10.3390/plants10102220 · Cited by 39 · see citing works
Structure analysis and quality evaluation of plant‐based meat analogs
Fu, J., Sun, C., Chang, Y., Li, S., Zhang, Y., & Fang, Y. (2022) · Journal of Texture Studies · doi:10.1111/jtxs.12705 · Cited by 48 · see citing works
Formation of a transparent soy protein hydrogel: Controlled thermal aggregation of protein using glutaminase
Li, T., Yang, Y.-Q., Lv, D.-Y., Wang, G.-S., Guo, J., Wan, Z., & Yang, X.-Q. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110202 · Cited by 49 · see citing works
Developments of Plant-Based Emulsion-Type Sausage by Using Grey Oyster Mushrooms and Chickpeas
Mazumder, M. A. R., Sujintonniti, N., Chaum, P., Ketnawa, S., & Rawdkuen, S. (2023) · Foods · doi:10.3390/foods12081564 · Cited by 51 · see citing works
“Soy protein, particularly texturized soy protein, is the prime ingredient in structured plant proteins due to its abundance, low cost, texture that resembles meat after being hydrated, and high-quality amino acid composition [3].”
Background
Local Sources of Protein in Low- and Middle-Income Countries: How to Improve the Protein Quality?
Vissamsetti, N., Simon-Collins, M., Lin, S., Bandyopadhyay, S., Kuriyan, R., Sybesma, W., & Tomé, D. (2023) · Current Developments in Nutrition · doi:10.1016/j.cdnut.2023.102049 · Cited by 53 · see citing works
“Other plant protein PDCAAS include 0.9 for pea protein, 0.9 for mustard ﬂ our, 0.6 for rolled oats, and 0.65 for cooked beans [24, 25].”
BackgroundInfluential
Bioactive peptides and metabolic health: a mechanistic review of the impact on insulin sensitivity, lipid profiles, and inflammation
Hamadou, M. (2025) · Applied Food Research · doi:10.1016/j.afres.2025.101056 · Cited by 47 · see citing works
Wet-milled chickpea coproduct as an alternative to obtain protein isolates
Espinosa‐Ramírez, J., & Serna-Saldivar, S. O. (2019) · LWT · doi:10.1016/j.lwt.2019.108468 · Cited by 47 · see citing works
Production of Fish Analogues from Plant Proteins: Potential Strategies, Challenges, and Outlook
Zhong, C., Feng, Y., & Xu, Y. (2023) · Foods · doi:10.3390/foods12030614 · Cited by 47 · see citing works
“Soybean, one of the most common plants-protein sources for producing meat analogues, has a PDCAAS of 95% to 102% when untruncated depending on testing methods and soybean sources, mostly at a value of 100% after truncation [22,23].”
Background
A techno-economic model of mycoprotein production: achieving price parity with beef protein
Risner, D., McDonald, K. A., Jones, C., & Spang, E. S. (2023) · Frontiers in Sustainable Food Systems · doi:10.3389/fsufs.2023.1204307 · Cited by 46 · see citing works
Thermal acid hydrolysis modulates the solubility of quinoa protein: The formation of different types of protein aggregates
Li, B., Xie, Y., & Guo, Q. Q. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.109825 · Cited by 47 · see citing works
Animal board invited review: The contribution of red meat to adult nutrition and health beyond protein
Ruxton, C. H. S., & Gordon, S. (2024) · animal · doi:10.1016/j.animal.2024.101103 · Cited by 46 · see citing works
Rice bran meat analogs: Relationship between extrusion parameters, apparent properties and secondary structures
Xiao, Z., Jiang, R., Huo, J., Wang, H., Li, H., Su, S., Gao, Y., & Duan, Y. (2022) · LWT · doi:10.1016/j.lwt.2022.113535 · Cited by 45 · see citing works
Soy-based renoprotection
McGraw, N., Krul, E. S., Grunz‐Borgmann, E. A., & Parrish, A. R. (2016) · World Journal of Nephrology · doi:10.5527/wjn.v5.i3.233 · Cited by 46 · see citing works
Dairy, Plant, and Novel Proteins: Scientific and Technological Aspects
Liu, Y., Aimutis, W. R., & Drake, M. A. (2024) · Foods · doi:10.3390/foods13071010 · Cited by 47 · see citing works
Pisum sativum vs Glycine max, a comparative review of nutritional, physicochemical, and sensory properties for food uses
Fischer, E., Cachon, R., & Cayot, N. (2019) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2019.11.021 · Cited by 43 · see citing works
A soy, whey and caseinate blend extends postprandial skeletal muscle protein synthesis in rats
Butteiger, D. N., Cope, M. B., Liu, P., Mukherjea, R., Volpi, E., Rasmussen, B. B., & Krul, E. S. (2012) · Clinical Nutrition · doi:10.1016/j.clnu.2012.10.001 · Cited by 43 · see citing works
Bitter taste masking of enzyme‐treated soy protein in water and bread
Bertelsen, A. S., Laursen, A., Knudsen, T. A., Møller, S., & Kidmose, U. (2018) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8903 · Cited by 43 · see citing works
Production of Endotoxin-Free Microbial Biomass for Food Applications by Gas Fermentation of Gram-Positive H2-Oxidizing Bacteria
Nyyssölä, A., Ojala, L. S., Wuokko, M., Gopalacharyulu, P. V., Tamminen, A., Tsitko, I. V., Nordlund, E., & Lienemann, M. (2021) · ACS Food Science & Technology · doi:10.1021/acsfoodscitech.0c00129 · Cited by 40 · see citing works
Microalgae protein digestibility: How to crack open the black box?
Walle, S. V. D., Broucke, K., Baune, M., Terjung, N., Royen, G. V., & Boukid, F. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2181754 · Cited by 41 · see citing works
Replacing Animal Protein with Soy-Pea Protein in an “American Diet” Controls Murine Crohn Disease–Like Ileitis Regardless of Firmicutes: Bacteroidetes Ratio
Basson, A. R., Gomez-Nguyen, A., LaSalla, A., Buttó, L. F., Kulpins, D., Warner, A. N., Martino, L. D., Ponzani, G., Ösme, A., Rodriguez‐Palacios, A., et al. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa386 · Cited by 38 · see citing works
Nutritional Value and Volatile Compounds of Black Cherry (Prunus serotina) Seeds
García-Aguilar, L., Rojas‐Molina, A., Ibarra‐Alvarado, C., Rojas-Molina, J., Vázquez‐Landaverde, P. A., Vázquez, F. J. L., & Zavala-Sánchez, M. Á. (2015) · Molecules · doi:10.3390/molecules20023479 · Cited by 39 · see citing works
“0, which indicates that a protein provides adequate amounts of all the essential amino acids [31].”
Background
Modulating the gel properties of soy glycinin by crosslinking with tyrosinase
Isaschar-Ovdat, S., Davidovich‐Pinhas, M., & Fishman, A. (2016) · Food Research International · doi:10.1016/j.foodres.2016.06.018 · Cited by 38 · see citing works
Effect of the mycelium of oyster mushrooms on the physical and flavor properties of a plant-based beef analogue
Zhang, Z., Zang, M., Chen, J., Zhang, K., Wang, S., Li, D., Li, X., Liu, M., & Xiaoqian, P. (2024) · LWT · doi:10.1016/j.lwt.2024.116029 · Cited by 37 · see citing works
Impact of Different Enzymatic Processes on Antioxidant, Nutritional and Functional Properties of Soy Protein Hydrolysates Incorporated into Novel Cookies
Knežević‐Jugović, Z. D., Culețu, A., Mijalković, J., Duță, D. E., Stefanović, A. B., Šekuljica, N. Ž., Đorđević, V. B., & Antov, M. G. (2022) · Foods · doi:10.3390/foods12010024 · Cited by 36 · see citing works
“It appeared that all hydrolysates as well as SPC did not contain any limiting essential amino acids (EAA) since all AAS values were higher than 1 (Table 1), which was consistent with the fact that soy protein isolate, and concentrate have been regularly reported as good quality proteins [41].”
Result
Four Conventional Soybean [Glycine max (L.) Merrill] Seeds Exhibit Different Protein Profiles As Revealed by Proteomic Analysis
Gomes, L., Senna, R., Sandim, V., Silva-Neto, M. A. C., Perales, J., Zingali, R. B., Soares, M. R., & Fialho, E. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf404351g · Cited by 36 · see citing works
Canola Seed Protein: Pretreatment, Extraction, Structure, Physicochemical and Functional Characteristics
Zhu, H., Wang, L., Li, X., Shi, J., Scanlon, M. G., Xue, S. J., Nosworthy, M. G., & Vafaei, N. (2024) · Foods · doi:10.3390/foods13091357 · Cited by 35 · see citing works
Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin
Isaschar-Ovdat, S., Rosenberg, M., Lesmes, U., & Fishman, A. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.07.007 · Cited by 35 · see citing works
Spray drying process optimization: Drought resistant variety (W82) soymilk powder using response surface methodology (RSM)
Singh, P., Bilyeu, L., & Krishnaswamy, K. (2022) · LWT · doi:10.1016/j.lwt.2022.113760 · Cited by 33 · see citing works
Investigation of the nutritional quality of raw and processed Canadian faba bean (Vicia faba L.) flours in comparison to pea and soy using a human in vitro gastrointestinal digestion model
Martineau-Côté, D., Achouri, A., Pitre, M., Wanasundara, J. P. D., Karboune, S., & L’Hocine, L. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113264 · Cited by 33 · see citing works
Prospects to improve the nutritional quality of crops
Scharff, L. B., Saltenis, V. L. R., Jensen, P. E., Baekelandt, A., Burgess, A. J., Burow, M., Ceriotti, A., Cohan, J., Geu‐Flores, F., Halkier, B. A., et al. (2021) · Food and Energy Security · doi:10.1002/fes3.327 · Cited by 33 · see citing works
“The mature seeds not only have a protein content of c. 37% (USDA, 2019a) but also provide sufficient quantities of all essential amino acids (Hughes et al., 2011).”
Background
Plant-Based Meat Analogues in the Human Diet: What Are the Hazards?
Gräfenhahn, M., & Beyrer, M. (2024) · Foods · doi:10.3390/foods13101541 · Cited by 32 · see citing works
“Although soy concentrates and isolates have PDCAAS values of 1.00 and DIAAS ≥ 75 [45,64], the gastric and intestinal in-vitro digestion of soy protein isolate leads to lower values of soluble nitrogen 74% and 66% compared to whey protein with 99% and 76%, respectively [65].”
BackgroundInfluential
Functional properties and Angiotensin-I converting enzyme inhibitory activity of soy–whey proteins and fractions
Lassissi, T. A., HETTIARACHCHY, N. S., Rayaprolu, S. J., Kannan, A., & Davis, M. E. (2014) · Food Research International · doi:10.1016/j.foodres.2014.07.015 · Cited by 31 · see citing works
Nutrikinetics of Isoflavone Metabolites After Fermented Soybean Product (Cheonggukjang) Ingestion in Ovariectomized Mice
Lee, D., Kim, M. J., Ahn, J., Lee, S. E., Lee, H.-J., Kim, J. H., Park, S., Jang, Y. J., Ha, T. Y., & Jung, C. H. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700322 · Cited by 30 · see citing works
Nutritional quality evaluation of commercial protein supplements
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Values for digestible indispensable amino acid scores (DIAAS) for some dairy and plant proteins may better describe protein quality than values calculated using the concept for protein digestibility-corrected amino acid scores (PDCAAS)
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The Protein Digestibility–Corrected Amino Acid Score Method Overestimates Quality of Proteins Containing Antinutritional Factors and of Poorly Digestible Proteins Supplemented with Limiting Amino Acids in Rats
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Nutrient Requirements and Interactions The Protein Digestibility–Corrected Amino Acid Score Method Overestimates Quality of Proteins Containing Antinutritional Factors and of Poorly Digestible Proteins Supplemented with Limiting Amino Acids
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The Protein Digestibility-Corrected Amino Acid Score (PDCAAS)—A Concept for Describing Protein Quality in Foods and Food Ingredients: A Critical Review
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Digestible indispensable amino acid scores for food proteins
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Authors: Hughes, G. J., Ryan, D. J., Mukherjea, R., & Schasteen, C. S.
Affiliations: Solae, LLC, 4300 Duncan Avenue, St. Louis, Missouri 63110, United States
Corresponding author: Hughes, Glenna J.
ORCID: Mukherjea, Ratna
Venue: Journal of Agricultural and Food Chemistry
Publisher: American Chemical Society (ACS)
Published: 2011-11-16
Volume: 59
Issue: 23
Pages: 12707-12712
ISSN: 0021-8561 (ISSN-L)
1520-5118
DOI: 10.1021/jf203220v
OpenAlex: W2023435153
Cited by: 316
References: 14
Citations by year: 2026: 24 · 2025: 35 · 2024: 35 · 2023: 66 · 2022: 37 · 2021: 30 · 2020: 24 · 2019: 17 · 2018: 10 · 2017: 8 · 2016: 11 · 2015: 5 · 2014: 6 · 2013: 4 · 2012: 4
FWCI: 6.54
Type: journal article
Language: en
Open access: closed
Locations: Journal of Agricultural and Food Chemistry (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords: PDCAAS, soy protein isolate, soy protein concentrate, protein quality, essential amino acids, true digestibility, amino acid composition, interlaboratory reproducibility, plant proteins
MeSH terms: Amino Acids, Amino Acids, Essential, Child, Preschool, Dietary Proteins, Digestion, Humans, Nutritive Value, Reference Values, Soybean Proteins

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Protein digestibility-corrected amino acid scores (PDCAAS) for soy protein isolates and concentrate: Criteria for evaluation

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