Mung Bean Protein (Vigna radiata)
Mung bean protein is a plant protein extracted from the seeds of the mung bean (Vigna radiata) and sold as an isolate, with tested isolates holding about 84 to 92 percent protein, used in plant-based egg substitutes and protein powders. It is relatively rich in leucine and lysine but low in the sulfur amino acids methionine and cysteine. The human evidence is small. In an 8-week trial in vegetarians, a mung bean egg-replacement patty did not change lean mass or any single strength test versus a lower-protein biscuit. A maker-funded isolate taken at 3 g a day did not lower fasting glucose but changed insulin and triglyceride markers mainly in a subgroup, and a 6-week drink trial raised a blood vessel function marker. No trial has tested muscle gain with training or weight loss. Mung bean protein may cause reactions in people allergic to birch pollen, soy, peanut or lupin.
Benefits
Plant protein source with a measured amino acid profile
In one commercial isolate, each gram of protein supplied 85.8 mg of leucine and 70.7 mg of lysine, above the reference pattern for children aged 3 to 10, but only 16.7 mg of methionine plus cysteine, the one group below it, giving a rat-based protein quality score of about 0.6.
Muscle strength in an 8-week feeding trial in vegetarians
In 25 underactive vegetarian adults who finished an 8-week trial, a mung bean egg-replacement patty adding 18 g of protein a day did not change lean mass, grip strength or leg strength on any single test versus a 4 g protein biscuit. Averaged across the three strength tests, the change was +2.9 versus -2.6 percent (p = 0.05) after adjustment.
Fasting insulin and triglyceride markers with a mung bean protein isolate
In a maker-funded 8-week trial in 44 adults with raised fasting glucose and triglycerides, 3 g a day of a mung bean protein isolate did not lower fasting glucose versus casein. Insulin fell within the mung bean group, and insulin, HOMA-IR and triglyceride changes differed from casein only in a subgroup with higher insulin resistance.
Blood vessel function marker over 6 weeks
In a 6-week double-blind trial in 27 healthy adults aged 45 to 60, a drink with 10 or 15 g of mung bean protein a day raised flow-mediated dilation of the arm artery and lowered some blood inflammation markers versus a placebo drink. Blood pressure and body weight did not change. Only 9 people were in each group.
Milk-free protein used in plant-based egg substitutes
Mung bean protein isolate is used as an egg and dairy replacer: the FDA had no questions about its use as a protein source in baked goods, dairy analogs, beverages and other foods, and the feeding trial in vegetarians used an egg-replacement patty made from mung bean. It is a legume protein, so it is not suitable for people allergic to it.
Mechanism of action
Amino acid supply and the leucine signal
Eating protein raises blood essential amino acids, and leucine helps switch on muscle protein synthesis. Mung bean protein isolate is fairly rich in leucine (85.8 mg per g of protein in one isolate), but methionine and cysteine fall short of requirement, so a serving delivers less of a complete amino acid supply than its total protein suggests. No study has measured muscle protein synthesis after mung bean protein.
Digestibility of mung bean protein
In healthy adults, true ileal digestibility of indispensable amino acids from cooked whole mung beans was 63 percent, rising to 71 percent after dehulling, lower than chickpea or yellow pea; tryptophan digestibility was 68 to 75 percent against about 90 percent for egg. These figures are for whole beans; a rat test of an isolate found about 95 to 97 percent fecal digestibility.
8S globulin, the main storage protein
About 80 percent of the protein in one commercial isolate is 8S globulin, a vicilin-type storage protein that resembles soy beta-conglycinin. The isolate's maker proposed that this protein drives effects on insulin and triglycerides seen in its trials; this rests on rat work and has not been shown as a mechanism in people.
Clinical trials
Randomized, participant-blinded parallel trial (registered NCT04076982, posted after completion) of a mung bean egg-replacement patty (JUST Egg; 18 g protein a day) versus an energy-matched biscuit (4 g protein a day) for 8 weeks without an exercise program; the registered primary outcomes were grip and leg strength, with lean body mass secondary. Funded by Arizona State University sources; the patties were donated by JUST, Inc. (Bartholomae et al. 2019, Nutrients)
37 healthy, underactive vegetarian and vegan adults aged 18 to 55 (34 women); 25 completed (11 mung bean, 14 control).
Lean body mass (p = 0.598), grip strength (p = 0.409), knee flexor (p = 0.211) and knee extensor strength (p = 0.153) did not differ between groups. The average percent change across the three strength tests was +2.9 percent with mung bean versus -2.6 percent with control (p = 0.05) after adjustment for body mass and adherence. Body weight change did not differ.
Two double-blind, casein-controlled trials of GLUCODIA mung bean protein isolate in chewable candies taken before breakfast and dinner: a 4-week dose-finding study of 1.5, 3 or 6 g a day and an 8-week main study of 3 g a day. No primary outcome or trial registry number is stated. Funded by Fuji Oil Holdings, the maker; four of the five authors were Fuji Oil staff (Kohno et al. 2018, J Nutr Sci)
Dose-finding: 29 adults analyzed (BMI 25 to 40, fasting glucose 110 to 125 mg/dl). Main study: 50 adults enrolled and 44 completed (BMI 25 to 35, fasting glucose 100 to 125 mg/dl, triglycerides 120 to 300 mg/dl).
In the dose-finding study, 3 and 6 g a day lowered fasting glucose versus casein. In the main study, fasting glucose did not change; insulin fell within the mung bean group (14.9 to 10.8 µU/ml) and the change in adiponectin differed from casein, though baseline adiponectin already differed. Insulin, HOMA-IR, triglyceride and ALT changes differed from casein only in a subgroup with HOMA-IR of 1.7 or more. Body composition did not differ.
Three-arm randomized, double-blind, placebo-controlled parallel trial (registered TCTR20230610002) of a daily drink with 10 or 15 g of a mung bean protein concentrate, or a matched placebo drink without it, for 6 weeks; both drinks also held mung bean and soy powder. Endothelial function by flow-mediated dilation was the main measure. Funded by Khon Kaen University and Thailand's National Science Research and Innovation Fund (Muchimapura et al. 2024, Foods)
29 healthy adults aged 45 to 60 with normal BMI recruited and 27 completed (9 per group; 25 women).
Flow-mediated dilation rose more with both mung bean doses than with placebo, and NF-kB, TNF-alpha and IL-6 were lower than with placebo. Nitrite, nitrate and nitric oxide fell only with 10 g. MDA and catalase did not differ, and blood pressure, heart rate and body weight did not change. Blood vessel and blood markers in a very small trial.
Dual stable isotope study (registered CTRI/2017/11/010468) in which intrinsically labeled, soaked and pressure-cooked legumes were eaten in a rice meal over 8 hours, referenced to labeled spirulina protein; whole and dehulled mung beans were compared in the same people. A single-meal digestibility measure of whole beans, not an isolate. Funded by the Wellcome Trust/DBT India Alliance and the IAEA (Kashyap et al. 2019, Am J Clin Nutr)
Healthy Indian adults with normal BMI (6 per legume; 6 in the whole versus dehulled mung bean comparison).
True ileal indispensable amino acid digestibility was 63.2 percent for whole mung bean against 71.6 percent for yellow pea and 74.6 percent for chickpea; dehulling raised mung bean to 70.9 percent. Threonine was the least digestible amino acid in whole mung bean (42 percent).
Dual stable isotope analysis of banked samples from earlier single-meal digestibility studies of intrinsically labeled plant and animal proteins, referenced to labeled spirulina protein. A digestibility marker of whole beans, not an isolate; funding is not stated in the abstract (Kashyap et al. 2024, J Nutr)
Healthy adults: 6 each for whole and dehulled mung bean, 5 to 7 for each other protein.
True tryptophan digestibility was 67.6 percent for whole mung bean and 74.5 percent for dehulled mung bean, against 89.7 percent for egg white, 91.4 percent for whole egg and 95.9 percent for chicken. Plant sources were significantly lower than animal sources, and tryptophan was not the limiting amino acid in any of them.
Side effects and drug interactions
Common Potential side effects
Important Drug interactions
Frequently asked questions about Mung Bean Protein (Vigna radiata)
Is mung bean protein a complete protein?
It contains all the essential amino acids, and is fairly rich in leucine and lysine, but it is low in the sulfur amino acids methionine and cysteine, which fell below requirement in EFSA's review of one isolate. In people, amino acids from cooked whole mung beans were less digestible than those from chickpea or pea.
Can mung bean protein help build muscle?
Not shown. In an 8-week trial in underactive vegetarians, a mung bean egg-replacement patty adding 18 g of protein a day did not change lean mass or any single strength test versus a lower-protein biscuit; only an averaged strength change differed. No study has measured muscle protein synthesis or tested mung bean protein with resistance training.
Who should avoid mung bean protein?
Anyone allergic to mung beans, and people allergic to soy, peanut, lupin or birch pollen unless an allergist says otherwise. EFSA said the protein could cause reactions in these groups, and in people with birch pollen allergy, reactions to mung bean sprouts are linked to an allergen that cross-reacts with birch and soy proteins.
Is mung bean protein approved as a food ingredient?
In the US, mung bean protein isolate was the subject of GRAS notice GRN No. 684, and in 2017 the FDA said it had no questions about its use as a protein source in baked goods, dairy analogs, beverages and other foods. In the EU, EFSA judged an isolate safe as a novel food ingredient in 2021.
Does mung bean protein help with weight loss?
Not shown. No trial has tested it for weight loss. Body weight did not change differently from control in the 8-week strength trial or the 6-week drink trial, and body composition did not differ from casein in the 8-week trial of a mung bean protein isolate.
What is Mung Bean Protein?
Mung bean protein is a plant protein extracted from the seeds of the mung bean (Vigna radiata) and sold as an isolate, with tested isolates holding about 84 to 92 percent protein, used in plant-based egg substitutes and protein powders.
What is Mung Bean Protein used for?
NutraSmarts does not list Mung Bean Protein under a health category. What the research covers: In one commercial isolate, each gram of protein supplied 85.8 mg of leucine and 70.7 mg of lysine, above the reference pattern for children aged 3 to 10, but only 16.
What is the recommended dosage of Mung Bean Protein?
No dose is established for any health outcome. Trials gave 18 g a day of protein from a mung bean egg-replacement patty for 8 weeks, 10 or 15 g a day in a drink for 6 weeks, and 1.5 to 6 g a day of an isolate (Glucodia) in candies for 4 to 8 weeks. Always follow the product label and check with a healthcare provider for personal advice.
Is Mung Bean Protein safe, and does it have side effects?
Side effects and cautions reported for Mung Bean Protein include: Allergy: EFSA concluded that mung bean protein may cause allergic reactions in people allergic to soybean, peanut, lupin or birch pollen. In patients with birch pollen allergy who reacted to mung bean sprouts, most had IgE to the mung bean allergen Vig r 1, which cross-reacts wit… It may also interact with some medications. Mung Bean Protein is not right for everyone, so check with a healthcare provider first if you are pregnant or breastfeeding, have a medical condition, or take prescription medication.
Does Mung Bean Protein interact with any medications?
Possible interactions include: Levodopa (with carbidopa): MedlinePlus advises talking to your doctor before changing to a high-protein diet; regular protein powder use adds to dietary protein. No other drug interactions specific to mung bean protein are documented in the sources cited here. If you take prescription medication, check with a pharmacist or doctor before using it.
How strong is the scientific evidence for Mung Bean Protein?
NutraSmarts rates the evidence for Mung Bean Protein as Limited (2 out of 5). It is backed by 5 study summaries and 13 cited references summarized on this page. A higher rating reflects more, larger, and better-designed human studies.
References(13 citations)
Evidence ratings on NutraSmarts are based on the totality of human clinical research, with emphasis on randomized controlled trials, meta-analyses, and systematic reviews. The references below directly support claims made throughout this page.
- Mung Bean Protein Supplement Improves Muscular Strength in Healthy, Underactive Vegetarian Adults. Nutrients. 2019;11(10):2423. doi: 10.3390/nu11102423.PubMedUsed to support: Randomized, participant-blinded 8-week feeding trial (NCT04076982, registered after completion) in 37 underactive vegetarian and vegan adults (34 women); 25 completed. A mung bean egg-replacement patty (JUST Egg; 18 g protein a day) was compared with an energy-matched biscuit (4 g protein a day). The registered primary outcomes, grip and leg strength, and lean body mass did not differ between groups on any single measure; the average percent change across the three strength tests was +2.9 versus -2.6 percent (p = 0.05) after adjustment for body mass and adherence. Body weight change did not differ. Funded by Arizona State University sources; the product was donated by JUST, Inc.
- Improvement of glucose and lipid metabolism via mung bean protein consumption: clinical trials of GLUCODIA™ isolated mung bean protein in the USA and Canada. J Nutr Sci. 2018;7:e2. doi: 10.1017/jns.2017.68.PubMedUsed to support: Two double-blind, casein-controlled trials of GLUCODIA mung bean protein isolate (92 percent protein; 8S globulin is 80 percent of the protein) given in chewable candies, funded by the maker, Fuji Oil Holdings. In a 4-week dose-finding study (29 analyzed), 3 and 6 g a day lowered fasting glucose versus casein. In the 8-week main study (50 enrolled, 44 completed) of 3 g a day in adults with raised fasting glucose and triglycerides, fasting glucose did not change; fasting insulin and HOMA-IR fell within the mung bean group, and the change in adiponectin differed from casein although baseline adiponectin already differed between groups. In a subgroup with HOMA-IR of 1.7 or more, changes in insulin, HOMA-IR, triglycerides and ALT differed from casein. Body composition did not differ. No primary outcome or registry number is stated; adverse events were mild.
- Mung Bean Functional Protein Enhances Endothelial Function via Antioxidant Activity and Inflammation Modulation in Middle-Aged Adults: A Randomized Double-Blind Trial. Foods. 2024;13(21):3427. doi: 10.3390/foods13213427.PubMedUsed to support: Three-arm randomized, double-blind, placebo-controlled trial (TCTR20230610002) in 27 healthy adults aged 45 to 60 (9 per group, 25 women) given a drink with 10 or 15 g of mung bean protein a day or a placebo drink for 6 weeks. Flow-mediated dilation of the brachial artery, the measure the trial was built around, rose more with both mung bean doses than with placebo, and blood NF-kB, TNF-alpha and IL-6 were lower than with placebo; MDA, catalase, blood pressure and body weight did not differ. Blood vessel and blood markers in a small trial. Funded by Khon Kaen University and Thailand's National Science Research and Innovation Fund; no conflicts declared.
- True ileal digestibility of legumes determined by dual-isotope tracer method in Indian adults. Am J Clin Nutr. 2019;110(4):873-882. doi: 10.1093/ajcn/nqz159.PubMedUsed to support: Dual stable isotope study (CTRI/2017/11/010468) in healthy Indian adults eating soaked, pressure-cooked legumes in a rice meal: true ileal indispensable amino acid digestibility was 63.2 percent for whole mung bean, 70.9 percent for dehulled mung bean (paired, n = 6), 71.6 percent for yellow pea and 74.6 percent for chickpea. In whole mung bean, threonine was the least digestible (42 percent). Whole cooked beans, not a protein isolate. Funded by the Wellcome Trust/DBT India Alliance and the IAEA.
- True Digestibility of Tryptophan in Plant and Animal Protein. J Nutr. 2024;154(11):3203-3209. doi: 10.1016/j.tjnut.2024.09.014.PubMedUsed to support: Dual isotope study in healthy adults using banked samples: true tryptophan digestibility was 67.6 percent for whole mung bean (n = 6) and 74.5 percent for dehulled mung bean (n = 6), against 89.7 percent for egg white and 91.4 percent for whole egg; plant sources were significantly lower than animal sources, and tryptophan was not a limiting amino acid in any tested protein. Whole beans, not an isolate.
- Measurement of protein digestibility in humans by a dual-tracer method. Am J Clin Nutr. 2018;107(6):984-991. doi: 10.1093/ajcn/nqy062.PubMedUsed to support: Methods paper (CTRI/2017/11/010468) developing a dual stable isotope test of protein digestibility in humans. In the legume test, done in one participant, average indispensable amino acid digestibility was 57.7 percent for intrinsically labeled whole mung bean protein, and dehulling raised it by 9.9 percent. Supported by the Wellcome Trust/DBT India Alliance.
- An observational study on the true indispensable amino acid digestibility of legume protein in infants. Am J Clin Nutr. 2025;122(6):1636-1640. doi: 10.1016/j.ajcnut.2025.09.027.PubMedUsed to support: Cross-sectional dual isotope study (CTRI/2020/09/027639) in 6 healthy infants aged 10 to 12 months: mean true indispensable amino acid digestibility of mung bean protein was 83.6 percent (SD 23.0), higher than the 63.2 percent measured earlier in adults, but the estimated DIAAS of mung bean protein at this age was 50 percent.
- Safety of mung bean protein as a novel food pursuant to Regulation (EU) 2015/2283. EFSA J. 2021;19(10):e06846. doi: 10.2903/j.efsa.2021.6846.PubMedUsed to support: EFSA opinion on a mung bean protein isolate submitted by Eat Just, Inc.: made by aqueous extraction at slightly alkaline pH, acid precipitation with citric acid, neutralization, pasteurization and spray drying; batches held 88.2 to 90.6 percent protein, with 3 to 4 percent fat. Per g of protein it supplied 85.8 mg leucine, 70.7 mg lysine and 16.7 mg methionine plus cysteine, the only amino acids below the reference pattern; rat-based PDCAAS was 0.58 to 0.64. Lectins, phytic acid and tannins were higher than in mung bean flour but comparable to other foods. The Panel found it safe as a food ingredient at the proposed uses and said it may cause allergic reactions in people allergic to soybean, peanut, lupin or birch pollen.
- GRAS Notice Inventory: GRN No. 684, Mung bean protein isolate. FDA GRAS Notice Inventory. 2017;Notifier Hampton Creek, Inc.; closure date 2017 Aug 4. Web page, accessed 2026..SourceUsed to support: Not PubMed-indexed (FDA GRAS Notice Inventory page, accessed 2026). GRN No. 684 for mung bean protein isolate, notified by Hampton Creek, Inc. for use as a protein source in baked goods and baking mixes, beverages, breakfast cereals, dairy analogs, pasta and grain products, snack foods and other foods; FDA responded that it had no questions (closed August 4, 2017).
- Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1. Clin Exp Allergy. 2005;35(8):1049-55. doi: 10.1111/j.1365-2222.2005.02309.x.PubMedUsed to support: Study of 10 patients with allergic reactions to mung bean seedlings (sprouts) and birch pollen allergy: all were sensitized to the birch allergen Bet v 1 and 90 percent to the soy allergen Gly m 4; IgE against the mung bean allergen Vig r 1 was found in 80 percent, and IgE binding to Vig r 1 was blocked by soy Gly m 4 in six of six patients tested. Concludes that mung bean sprout allergy can follow primary sensitization to birch pollen.
- Vig r 6, the cytokinin-specific binding protein from mung bean (Vigna radiata) sprouts, cross-reacts with Bet v 1-related allergens and binds IgE from birch pollen allergic patients' sera. Mol Nutr Food Res. 2014;58(3):625-34. doi: 10.1002/mnfr.201300153.PubMedUsed to support: Laboratory study of sera: 73 and 32 percent of 60 birch-allergic patients sensitized to Bet v 1 had IgE binding to the mung bean allergens Vig r 1 and Vig r 6; among 19 patients with reactions or positive prick tests to mung bean sprouts, 79 and 63 percent did. Bet v 1 fully blocked IgE binding to both, supporting birch pollen cross-reactivity.
- Potential allergens of green gram (Vigna radiata L. Millsp) identified as members of cupin superfamily and seed albumin. Clin Exp Allergy. 2011;41(8):1157-68. doi: 10.1111/j.1365-2222.2011.03780.x.PubMedUsed to support: Mouse sensitization and patient sera study: in 12 patients with nasal and bronchial allergy sensitized to green gram (mung bean), four pepsin-resistant seed proteins bound IgE (Vig r 2 to Vig r 5); Vig r 2 and Vig r 3 were identified as 8S globulin isoforms and Vig r 4 as a seed albumin, with sequence similarity to allergens of soybean, lentil, pea and lupin. Supports the allergy note for seed (not only sprout) proteins.
- Levodopa and Carbidopa: MedlinePlus Drug Information MedlinePlus. 2026;Web page, accessed 2026..SourceUsed to support: Not PubMed-indexed (NIH web page, accessed 2026). Advises patients taking levodopa and carbidopa to talk to their doctor if they plan to change to a diet high in protein.