Pea

Pea (Pisum sativum L.): A Comprehensive Reference

1. Identity

Botanical and Chemical Names

The pea (Pisum sativum L.) is a herbaceous annual plant in the family Fabaceae, grown virtually worldwide for its edible seeds. It belongs to the Leguminosae family, which includes 800 genera and 20,000 species of plants, and is a diploid plant (2n = 14) with a short vegetation period. Informal synonymy: Grokipedia notes that some recent genomic reclassifications have proposed the garden pea also be listed under Lathyrus oleraceus Lam., though Pisum sativum L. remains the overwhelmingly dominant accepted name in agriculture, nutrition science, and regulatory contexts.

Plant Description and Natural Source

The plant exhibits a climbing or trailing growth habit, reaching 0.5–2 metres in height depending on variety, supported by slender tendrils. The compound leaves bear two to three pairs of ovate leaflets that terminate in coiling tendrils, and flowers — typically white or pink-purple — are borne singly or in pairs on short peduncles, giving rise to pods 5–10 cm long containing 4–10 round seeds. The wild plant is native to the Mediterranean region, and ancient remains dating to the late Neolithic Period have been found in the Middle East.

Cultivar Groups and Commercial Forms

Whole peas, commonly referred to as dry, green, or field pea, constitute one of the most common and economically important legumes. Some varieties, including sugar peas and snow peas, produce pods that are edible and are eaten raw or cooked like green beans; they are popular in East Asian cuisines. As a dietary supplement and functional food ingredient, pea is commercially available in several forms:

• Whole dried peas: The traditional form, used in soups, porridges, and dals.
• Pea flour: Ground whole or dehulled dried peas, retaining fiber, starch, and protein.
• Pea protein concentrate (PPC): Produced by removing a portion of starch and fiber, typically containing 55–70% protein by dry weight.
• Pea protein isolate (PPI): A highly processed form produced by alkaline extraction and isoelectric precipitation, typically containing ≥80–90% protein by dry weight; the dominant form in sports nutrition supplements.
• Pea protein hydrolysate (PPH): An enzymatically digested form generating shorter peptides with specific bioactivities, including ACE-inhibitory and antidiabetic peptides.
• Pea fiber concentrate: Isolated from the hull or cotyledon fraction; used in fiber-fortified food products.
• Pea starch: Isolated starch fraction, valued for its resistant starch content.

Industrial development followed a clear timeline: early agricultural use as a staple legume gave way to biochemical descriptions of seed proteins in the 1830s–1930s, and industrial fractionation methods (alkaline extraction and isoelectric precipitation) were applied to legumes from the 1970s–1990s, with growth in plant-based protein demand and optimization of isolates for flavor, solubility, and nutrition accelerating from the 2000s to the 2020s.

2. Traditional and Historical Use

Ancient Origins and Archaeological Evidence

Peas (Pisum sativum L.) have been domesticated for over 6,000 years, with archaeological evidence including 9,000-year-old carbonized seeds from Neolithic sites in Turkey. Archaeological evidence suggests that peas were cultivated in the Fertile Crescent as early as 9,000 years ago, and excavations at sites such as Jericho in modern-day Israel and Çayönü in southeastern Turkey have uncovered evidence of pea cultivation, including charred pea pods and seeds. Primitive garden peas have also been found during excavations beneath houses of Swiss lake dwellers at Morssedorf dating back to both the Bronze and Stone Age, and peas were found in a Hungarian cave dwelling believed to date back even further.

Spread and Diversification

Ancient Greek and Roman texts confirm early cultivation in Europe; following domestication, peas spread northwestward across southern Europe, and historical records suggest their introduction to India predated Persian and Greek influence in the region. In China, peas were cultivated as early as the Han Dynasty (206 BCE–220 CE), where they were considered a delicacy used in traditional medicine; in India, peas were an important crop in the Indus Valley Civilization (3300–1300 BCE), where they were incorporated into curries and other dishes. Initially cultivated for dried seeds, pea consumption shifted during the Middle Ages with the emergence of podded vegetable varieties; archaeological remains from 9th–11th century Swedish tombs and 18th-century Dutch records document this transition, with vegetable peas introduced to England circa 1760.

Traditional Medicinal and Culinary Preparations

Culinarily, peas appear in traditional dishes across Europe, Asia, and the Middle East, often associated with seasonal harvests and regional cuisines. Dried peas were historically significant as a stored food source, while fresh peas became associated with springtime and early harvest periods. Ancient Greek and Roman texts reference peas as nourishing and restorative, while Traditional Chinese Medicine utilized peas to support digestion and promote fluid balance. In European folk medicine, peas were sometimes mashed and applied as poultices to soothe skin irritations, minor wounds, or inflammation, owing to their gentle astringency and emollient qualities. Peas were also valued as a reliable remedy against malnutrition and scurvy in times of scarcity.

Theophrastus — considered by many to be the Father of Botany — described peas and their cultivation in detail in his Enquiry into Plants, in the chapter devoted to cereals and peas. In the mid-1800s, peas in a monastery garden in Austria were famously used by the monk Gregor Mendel in his pioneering studies of the nature of heredity.

It should be noted that the historical use of peas as a food and folk remedy was entirely centred on the whole food — dried, fresh, or cooked. The use of isolated pea protein, pea fiber, or pea starch as discrete dietary supplements is a modern, 21st-century development with no parallel in historical medicinal traditions.

3. Key Constituents and Active Compounds

Macronutrient Profile

Pea seeds typically contain 20%–40% protein, 45%–55% starch, and 10%–15% dietary fiber, alongside essential micronutrients such as vitamin C (40–60 mg/100 g), folate (60–70 μg/100 g), vitamin K (30–45 μg/100 g), iron (1.5–2.0 mg/100 g), and manganese (0.4–0.6 mg/100 g). Depending on cultivar, peas contain lipid (0.57–3.52%), dietary fiber (11.34–16.13%), soluble sugar (17.53–23.99%), protein (19.75–26.48%), and starch (32.56–48.57%).

Mineral Content

A 100 g serving of peas provides the following average percent daily value based on U.S. recommendations: 8% Ca, 39% Mg, 73% Cu, 37% Fe, 63% Mn, 45% Zn, 28% K, and 43% P.

Protein Fractions

Pea protein predominantly comprises three main globulin fractions: vicilin (7S), legumin (11S), and convicilin, accompanied by albumins. Globulins constitute the majority of pea protein (65–85%), predominantly consisting of the high-molecular-weight 11S legumin and the lower-molecular-weight 7S vicilin and convicilin. Vicilin and legumin together constitute approximately 80–90% of the total pea seed protein, with varying ratios among cultivars affecting functional behavior. Pea protein is made up of approximately 15%–25% pea albumin and 50%–60% pea globulin, with a high lysine and tryptophan content.

Legumin is a hexameric protein with a compact quaternary structure stabilized by electrostatic, disulfide, and hydrophobic interactions, having a molecular weight of 320–400 kDa with a beta-sheet-rich structure. The mature protein contains six subunits, each subunit pair consisting of an acidic (40 kDa) and a basic (20 kDa) chain linked by a single disulfide bond; the hydrophilic α-chains are on the molecule's surface while hydrophobic sections are immersed in the inner surface.

The protein fraction in peas is primarily composed of globulins (legumin and vicilin) and albumins, which are storage proteins with relatively high nutritional value. Pea proteins are especially rich in the essential amino acids lysine and arginine, though they are relatively low in sulfur-containing amino acids such as methionine and cysteine — a key distinction from dairy proteins.

Bioactive Compounds and Phytochemicals

Ethanol extracts of pea cultivars contain approximately 12 kinds of phenolic substances and show antioxidant activities on DPPH radical scavenging, ferric reducing antioxidant power (FRAP), and oxygen radical absorbance capacity (ORAC); phenolic content and protocatechuic acid show a positive correlation with antioxidant capacity.

Peas are also rich in fiber components (hull fiber, resistant starch, and oligosaccharides), carbohydrate, ferritin, vitamins, minerals, and phytochemicals. Key phytochemical classes identified in Pisum sativum include flavonoids (kaempferol, quercetin glycosides), carotenoids (lutein, zeaxanthin, β-carotene in green peas), and chlorophylls.

Bioactive Peptides

Antihypertensive peptides from pea protein are typically characterized as inhibitors of angiotensin I-converting enzyme (ACE), reflecting the essential role of the renin-angiotensin system in regulating blood pressure; another study reported that angiotensin-converting enzyme 2 activity from pea protein is considered a strategy for identifying antihypertensive capacity. Food proteins, including pea, have been recognized as an ideal source for releasing bioactive peptides with the potential to intervene in nutrition-related chronic diseases such as cardiovascular diseases, obesity, and diabetes.

Antinutritional Factors

The main antinutrients in peas are tannins, phytic acid, cyanogenic glycosides, saponins, oxalates, biogenic amines, lectins, protease inhibitors, and amylase inhibitors; the most concerning metabolites are phytic acid, tannins, and trypsin inhibitors. These components interfere with the nutritional value of foods by reducing mineral absorption and protein digestibility, and by causing toxicity and health disorders when present at high concentrations. Phytic acid forms insoluble complexes with minerals like copper, iron, and zinc, reducing their bioavailability in the human gastrointestinal tract.

The digestibility of legume seed proteins is hindered by the protein structure and, to a greater extent, by other components within the seed matrix such as trypsin inhibitors, phytates, tannins, and lectins; trypsin inhibitors act on proteases — or, like phytates and tannins, form insoluble and indigestible complexes with proteins — altering protein structures and limiting protease activity.

4. Mechanisms of Action

Protein Synthesis and Muscle Anabolism

Studies have shown that an increased plasma concentration of leucine favours muscle protein synthesis and that its action on muscle mass is potentiated by the presence of other amino acids such as those contained in pea protein. Therefore, pea protein could contribute to muscle protein synthesis when taken immediately after effort, and these arguments suggest that pea protein ingestion might maximize muscle mass gains during resistance training.

Blood Pressure Regulation (ACE Inhibition)

Pea protein hydrolysate (PPH)-fed animals showed lower plasma levels of angiotensin II — the major vasopressor involved in development of hypertension — with no effect on plasma ACE activity or renal mRNA levels of ACE. Oral administration of unhydrolyzed pea protein isolate had no blood pressure-reducing effect, suggesting that thermolysin hydrolysis is responsible for releasing the bioactive peptides from the native protein. Renal expression of renin mRNA levels was reduced by approximately 50% in PPH-fed animals, suggesting that reduced renin may be responsible for the reduced blood pressure.

Glycemic and Insulinemic Mechanisms

The associated mechanisms of pea protein hydrolysate's hypoglycemic effects include suppression of the gluconeogenic pathway, activation of the insulin signaling pathway, and modulation of the renin-angiotensin system in the liver of diabetic animals. Dietary fiber from peas contributes to blood glucose management through mechanisms including delayed nutrient absorption, increased satiety, and stimulation of gut hormones that regulate food intake; fiber may also beneficially modulate the intestinal microbiota, which influences whole-body energy metabolism.

Satiety and Appetite Regulation

Fiber is a critical aspect of the diet because of its beneficial effects on numerous risk factors, including reducing plasma lipid levels, improving glucose metabolism, and enhancing satiety, which helps to reduce food intake. Dietary fiber produces short-chain fatty acids (SCFAs) through intestinal microbial fermentation, while promoting the secretion of glucagon-like peptide 1 (GLP-1) and peptide YY (PYY).

5. Scientific Evidence by Area of Use

5.1 Skeletal Muscle: Strength and Hypertrophy

The most robust clinical evidence for pea-derived supplementation relates to its use as a protein source in combination with resistance exercise training.

Key RCT (Babault et al., 2015): A double-blind, randomized, placebo-controlled clinical trial compared the impact of oral supplementation with pea protein (NUTRALYS®) vs. whey protein and placebo on biceps brachii muscle thickness and strength after a 12-week resistance training program. 161 males aged 18–35 years were enrolled and underwent 12 weeks of resistance training on upper limb muscles; according to randomization, they were included in the pea protein (n=53), whey protein (n=54), or placebo (n=54) group. All participants took 25 g of the proteins or placebo twice daily during the 12-week training period. Supplementation with pea protein promoted a greater increase of muscle thickness compared to placebo, particularly for people starting or returning to muscular strengthening; since no difference was obtained between the two protein groups, vegetable pea proteins could be used as an alternative to whey-based dietary products.

RCT (PMC, 2024): Sedentary adults were randomized to pea protein or whey protein in combination with a weekly resistance training program for 84 days; changes in whole-body muscle strength (WBMS) including handgrip, lower body, and upper body strength, body composition, and product perception were assessed. There were no significant differences in the change in WBMS, muscle mass, or product perception scores between the pea protein and whey groups. Participants supplemented with pea protein had a 16.1% improvement in WBMS following 84 days of supplementation (p=0.01), while those taking whey protein had an improvement of 11.1% (p=0.06). Eighty-four days of pea protein supplementation resulted in improvements in strength and muscle mass comparable to whey protein when combined with a resistance training program in a population of healthy sedentary adults; pea protein may be considered a viable alternative to animal-sourced whey protein without sacrificing muscular gains.

Evidence strength: Moderate. Multiple RCTs consistently show pea protein is non-inferior to whey protein for muscle hypertrophy and strength gains when used with resistance training. Limitations include: industry funding for the 2015 Babault trial, use of proprietary pea protein preparations, absence of dietary protein controls, and a predominantly male study population. Large-scale independent replication is needed.

5.2 Cardiovascular Health: Blood Pressure

Animal/pre-clinical evidence: Oral administration of pea protein hydrolysate to spontaneously hypertensive rats at doses of 100 and 200 mg/kg body weight led to a lowering of hourly systolic blood pressure, with a maximum reduction of 19 mmHg at 4 hours; unhydrolyzed pea protein isolate had no blood pressure-reducing effect. Oral administration of pea protein hydrolysate over an 8-week period to an animal model of chronic kidney disease led to 29 and 25 mmHg reductions in systolic and diastolic blood pressure, respectively.

Evidence strength: For blood pressure specifically, the available evidence at the level of human clinical trials is limited and preliminary. The animal data for ACE-inhibitory pea peptides is promising, but robust, adequately powered human RCTs demonstrating clinically meaningful antihypertensive effects of pea protein hydrolysate are not yet available in quantity. This area warrants further clinical investigation.

5.3 Glycemic Control and Metabolic Health

Human RCT (crossover, 2024–2025): A single-blind, randomised, crossover study compared the effects of co-ingesting glucose with 10 or 20 g of whey protein and glucose with 10 or 20 g of pea protein, with a reference product (glucose alone), on glycaemic and insulinaemic responses in 30 healthy individuals. Blood glucose and plasma insulin were measured at baseline, 15, 30, 45, 60, 90, 120, 150, and 180 minutes after product consumption. Glucose incremental area under the curve (iAUC) at 180 minutes was significantly reduced (p<0.001) for glucose with 20 g pea protein (89.8 ± 51.6 mmol/L·min) and glucose with 20 g whey protein (98.5 ± 58.0) compared to glucose alone (143.2 ± 74.0). Insulin iAUC at 180 minutes for glucose with 20 g pea protein was significantly lower (p<0.001) than glucose with 20 g whey protein.

Animal evidence: Pea protein hydrolysate administered orally at a dosage of 1000 mg/kg body weight for 9 weeks reduced fasting blood glucose by 29.6% and improved glucose tolerance in type 2 diabetic mice. In addition, the levels of pro-inflammatory markers in both liver and serum were reduced by pea protein hydrolysate treatment.

Pea fiber and glycemia: Incorporation of whole yellow pea flour into baked products reduced postprandial glycemia in healthy men and women compared to products containing whole wheat flour. In overweight hypercholesterolaemic adults, providing baked products containing pea fiber (12 g/day of fiber) for 28 days reduced fasting insulin concentrations and improved postprandial glucose responses after a standardised breakfast meal.

Evidence strength: Preliminary to moderate. Human evidence for glycaemic modulation exists across multiple study designs, but many trials are short-term, use small sample sizes, or apply pea fractions in composite food matrices making attribution difficult. Animal data on pea protein hydrolysate's antidiabetic mechanisms is mechanistically interesting but cannot be directly extrapolated to humans at standard supplemental doses.

5.4 Body Weight and Satiety

Human RCT (yellow pea fiber, 2016–2017): A double-blind, placebo-controlled, parallel group study assessed the effects of yellow pea fiber supplementation on weight loss in overweight and obese adults (BMI 25–38). Participants were randomized to either 15 g/day yellow pea fiber supplementation or an isocaloric placebo for 12 weeks (n=30/group). The primary outcome was change in body fat from baseline; secondary outcomes included glucose tolerance, appetite regulation, serum lipids, and inflammatory markers. The conclusion of this trial was that incorporating 15 g/day yellow pea fiber may yield small but significant metabolic benefits and aid in obesity management in the absence of other lifestyle changes.

Evidence strength: Preliminary. A single RCT of modest size showing small effects, with the authors themselves noting the limited state of evidence. Fiber-mediated satiety mechanisms (GLP-1, PYY, delayed gastric emptying) are biologically plausible but need larger, longer trials for confirmation in the context of pea-specific fiber products.

5.5 Gut Microbiome Modulation

Although the bioactive peptides of peas contribute to their health benefits, gut microbiome modulation by pea protein has more recently become of interest. Dietary fiber may also produce unique changes in gut microbiota, which independently may improve glucose tolerance, satiety, and lipid metabolism.

A randomized double-blinded crossover clinical study of pea protein blended with an enzymes-probiotics supplement showed changes with respect to Archaea and a few uncharacterised species but did not show statistically significant variations in microbiome profile at the higher taxonomic levels. A study with a large sample size and detailed gut microbiome analysis was warranted to confirm the results statistically and characterize altered species.

Evidence strength: Very preliminary. Human clinical evidence for pea-specific microbiome modulation is sparse, with available trials being underpowered or combining pea protein with other supplements such as probiotics and enzymes, making attribution to pea alone impossible. This is an active area of research.

5.6 Antioxidant Activity

Through UPLC-QTOF-MS and HPLC-QQQ-MS/MS analysis, ethanol extracts of pea cultivars include approximately 12 kinds of phenolic substances and show antioxidant activities on DPPH radical scavenging, ferric reducing antioxidant power (FRAP), and oxygen radical absorbance capacity (ORAC). Key research topics include dietary fibers, carotenoids, phenolic compounds, and antinutrients affecting mineral bioavailability.

Evidence strength: In vitro and cultivar characterisation studies predominate. Robust human clinical trials specifically attributing measurable antioxidant health benefits to pea consumption are not yet established.

6. Dosage Forms and Dosages Reported in Studies

The following dosages reflect those reported in peer-reviewed clinical research; they are not recommendations.

• Pea protein (muscle/strength trials): 25 g of pea protein taken twice daily (50 g/day total) for a 12-week resistance training program was the dosage used in the Babault et al. (2015) RCT. Sedentary adults were randomised to pea protein or whey protein in combination with a resistance training program for 84 days in the 2024 RCT, which used a comparable daily supplement protocol.
• Pea protein (glycaemic crossover trial): 10 or 20 g of pea protein co-ingested with glucose in a crossover design with 30 healthy individuals.
• Pea protein hydrolysate (animal, glycaemic): 1000 mg/kg body weight administered orally for 9 weeks in a mouse model of type 2 diabetes.
• Pea protein hydrolysate (animal, blood pressure): 100 and 200 mg/kg body weight in spontaneously hypertensive rats.
• Yellow pea fiber (weight/metabolic health): 15 g/day yellow pea fiber supplementation for 12 weeks in overweight and obese adults (BMI 25–38).
• Pea fiber (glycaemia/insulin in hypercholesterolaemic adults): 12 g/day of fiber from baked products containing pea fiber for 28 days.
• Pea protein (gut microbiome/amino acid absorption study): 20 g of pea protein (with or without Lactiplantibacillus plantarum TWK10) for 28 days combined with resistance exercise training three times per week.

7. Body Systems and Health Areas of Association

• Musculoskeletal system: Muscle protein synthesis, hypertrophy, and strength gains in combination with resistance training — the area with the strongest clinical evidence base.
• Cardiovascular system: ACE-inhibitory bioactive peptides (from hydrolysate fractions) with potential antihypertensive effects; lipid metabolism via pea fiber.
• Metabolic/endocrine system: Postprandial glycaemic modulation, insulin response attenuation, and antidiabetic mechanisms (animal data for hydrolysate).
• Gastrointestinal system: Fiber fermentation, SCFA production, gut hormone secretion (GLP-1, PYY), and putative microbiome modulation.
• Immune system: Pea protein is rich in lysine, which helps to maintain a healthy immune system.
• Antioxidant defense: Phenolic compounds and carotenoids with measurable in vitro radical-scavenging capacity.

8. Protein Quality: PDCAAS and DIAAS

The Protein Digestibility-Corrected Amino Acid Score (PDCAAS) has been used as a measure for assessing protein quality; U.S. labeling regulations indicate that a protein must have a PDCAAS value greater than 20% to qualify as a quality protein for non-infant foods, and greater than 40% for infant foods. While the PDCAAS value for soybean is 100%, the same for other legumes is 28–75%.

The Digestible Indispensable Amino Acid Score (DIAAS) is a newer approach to measuring protein quality of foods, supported by the Food and Agriculture Organization of the United Nations; methodological concerns about PDCAAS are addressed by DIAAS through the introduction of ileal amino acid digestibility coefficients and untruncated protein scores. Several foods from the categories seeds, nuts, and pulses — including yellow peas — would score differently under the DIAAS system compared to PDCAAS, a finding discussed in the context of Canadian and international food guidance. The primary limiting amino acid for pea protein is methionine (and to a lesser extent cysteine), a deficiency that can be addressed by combining pea protein with complementary plant sources (e.g., rice protein, which is higher in sulfur-containing amino acids).

9. Safety Considerations and Interactions

Antinutrients and Nutrient Bioavailability

Although peas contain a wide range of beneficial components, they also have certain anti-nutritional factors (also called non-nutrients) — such as phytic acid, lectins, and trypsin inhibitors — which can interfere with nutrient absorption. Despite these antinutrients reducing nutrient bioavailability, several recent studies have also highlighted their role as bioactive compounds due to their metabolic and physiological benefits. Phytates, which serve as reservoirs for phosphate and minerals in seeds, may also affect the absorption of zinc and iron from crops, potentially limiting their nutritional value.

Lectins can react with intestinal epithelial cells, altering intestinal permeability, resulting in intestinal hypertrophy and hyperplasia, and can cause harm to the lining of the digestive tract, particularly the small intestine, which may reduce protein digestibility. Standard cooking and processing methods substantially reduce or eliminate these concerns: fermentation is a processing technique that may lower the amount of phytate in pea protein isolates; for example, phytic acid levels of a pea-oat protein blend extruded meat analogue were decreased by 32% by enzymatic treatment and 18% by extrusion.

Allergenicity

Pis s 1 (vicilin), Pis s 2 (convicilin), and Pis s 3 (non-specific lipid transfer protein — nsLTP) belonging to legumin-like globulin proteins were identified as the allergens of pea, reported by and accepted as food allergens by the International Union of Immunological Sciences. Vicilin and convicilin are potential major allergens from pea seeds; furthermore, proteolytic fragments from vicilin are also relevant IgE-binding pea components. All of these proteins cross-react with the major lentil allergen Len c 1.

IgE immunodetection of crude pea extracts revealed that convicilin (63 kDa), as well as vicilin (44 kDa) and one of its proteolytic fragments (32 kDa), reacted with more than 50% of the individual sera tested in a study of 18 patients with pea allergy; additional proteolytic subunits of vicilin (36, 16, and 13 kDa) bound IgE from approximately 20% of the sera. Cross-reactivity between pea and other legumes (particularly peanut, lentil, and soybean) is a clinically relevant consideration for individuals with known legume allergies. Pea protein isolate is generally considered relatively hypoallergenic compared to dairy and soy proteins, but it is not allergen-free.

Tolerability

Both pea protein and whey protein study products were safe and well-tolerated in the enrolled population of the 2024 randomized clinical trial in sedentary adults. Gastrointestinal effects such as bloating and flatulence — common to high-fiber legume products — are a known but generally mild consideration with whole pea or pea-fiber supplementation, attributable to the fermentation of oligosaccharides (raffinose-family oligosaccharides) and resistant starch in the colon.

Interactions and Special Populations

The Food and Agriculture Organization of the United Nations (FAO) introduced an alternative measurement of protein quality named the Digestible Indispensable Amino Acid Score (DIAAS), which may better characterize pea protein's true contribution to essential amino acid needs in different populations. Pea protein's relatively high arginine content is of theoretical interest in contexts involving nitric oxide synthesis and vascular function, though specific human clinical evidence in this area is not yet well established. Individuals with chronic kidney disease and protein restriction should exercise caution with high-dose pea protein supplementation, as with any concentrated protein source. No well-characterized pharmacokinetic drug-nutrient interactions with pea protein isolate have been identified in the clinical literature to date.

References

• Nutritional composition and health benefits of peas — a bibliometric research (PubMed, 2025)
• Comprehensive analysis in the nutritional composition, phenolic species and in vitro antioxidant activities of different pea cultivars (PubMed, 2023)
• Peas, natural resources for a sustainable future: a multifaceted review (PMC, 2025)
• Nutritional Value Evaluation of New Pea Genotypes (Pisum sativum L.) Based on Their Chemical, Amino Acids and Dietary Fiber Composition (PMC, 2024)
• Characterization of pea seed nutritional value within a diverse population of Pisum sativum (PubMed, 2021)
• A Comprehensive Review of Pea (Pisum sativum L.): Chemical Composition, Processing, Health Benefits, and Food Applications (MDPI Foods, 2023)
• Pea proteins oral supplementation promotes muscle thickness gains during resistance training: a double-blind, randomized, placebo-controlled clinical trial vs. Whey protein (PMC/JISSN, 2015)
• Efficacy of Pea Protein Supplementation in Combination with a Resistance Training Program on Muscle Performance in a Sedentary Adult Population: A Randomized, Comparator-Controlled, Parallel Clinical Trial (PMC, 2024)
• Pea protein hydrolysate reduces blood glucose in high-fat diet and streptozotocin-induced diabetic mice (PMC, 2024)
• Blood pressure lowering effect of a pea protein hydrolysate in hypertensive rats and humans (PubMed/J Agric Food Chem, 2011)
• A randomized controlled trial in healthy participants to compare the insulinogenic effects of whey protein and pea protein co-ingested with glucose (PMC, 2025)
• The Current Situation of Pea Protein and Its Application in the Food Industry (PMC, 2022)
• Consuming yellow pea fiber reduces voluntary energy intake and body fat in overweight/obese adults in a 12-week randomized controlled trial (PubMed/Clin Nutr, 2017)
• Evaluation of yellow pea fibre supplementation on weight loss and the gut microbiota: a randomized controlled trial (BMC Gastroenterology, 2014)
• Pea Protein Isolates: From Extraction to Functionality (PMC, 2025)
• Vicilin and convicilin are potential major allergens from pea (PubMed/Clin Exp Allergy, 2004)
• A review on traditional technology and safety challenges with regard to antinutrients in legume foods (PMC, 2021)
• Legume Seed Protein Digestibility as Influenced by Traditional and Emerging Physical Processing Technologies (PMC, 2022)
• Study of amino acids absorption and gut microbiome on consumption of pea protein blended with enzymes-probiotics supplement (PMC/Front Nutr, 2024)
• Gut microbiota modulation and amino acid absorption by Lactiplantibacillus plantarum TWK10 in pea protein ingestion (PMC, 2024)
• Integrated agronomy of pea (Pisum sativum L.): a review on cultivation, harvesting, and storage (Frontiers in Plant Science, 2025)
• Pea | Origin, Variety & Cultivation (Encyclopædia Britannica)
• Potential impact of the digestible indispensable amino acid score as a measure of protein quality on dietary regulations and health (PMC, 2018)
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• Nutritional composition and health benefits of peas — a bibliometric research (PMC, 2025)