Lima bean

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Code: f182
Latin name: Phaseolus lunatus
Source material: Dried beans
Family: Fabaceae (Leguminosae)
Common names: Lima bean, Butter bean, Sugar bean, Haba bean, Pallar bean, Burma bean, Guffin bean, Hibbert bean, Sieva bean, Rangoon bean, Madagascar bean, Paiga, Paigya, Butterpea, Prolific bean, Civet bean

Allergen Exposure

Geographical distribution

Lima bean is a legume (1). Its seed is eaten as a vegetable. It is of Andean and Mesoamerican origin. The genus Phaseolus includes Lima, garden, snap, string, navy and pinto beans.

Lima plants produce pods that are up to 15 cm long and contain seeds that at maturity are 1 to 3 cm long and oval- to kidney-shaped. The seeds are usually quite flat but in some varieties are more spherical in shape. Immature seeds are uniformly green. At maturity, the most common variety produces white seeds, although black, orange, red and mottled seeds are seen.

"Butter bean" is the widespread term for a large, flat, white variety of Lima bean (P. lunatus var. macrocarpus, or P. limensis). In the southern United States, the smaller Sieva type are traditionally called Butter beans (or the Dixie or Henderson type). In that area, Lima beans and Butter beans are seen as 2 distinct types. In the United Kingdom, a "Butter bean" is a dried bean that can be re-hydrated, or a canned bean ready to use. In culinary terms, Lima beans and Butter beans are distinct, the former being small and green, the latter large and yellow (2).

Lima bean contains a number of anti-nutrients. Raw Lima beans contain cyanide, trypsin inhibitor, lectin, phytin and tannin. Soaking, autoclaving and toasting completely eliminated trypsin inhibitor and lectin, while it significantly reduced the levels of phytin, tannin and cyanide. Except for tannin, autoclaving for 20 minutes was found to eliminate all the other anti-nutrients in Lima bean (1). Lectin-related polypeptides are a class of defence proteins found in seeds of Phaseolus species, including in Lima bean (3). Lectins react indistinctly with erythrocytes of the ABO blood system; however, the lectin of Lima bean is specific to the blood group type A (4).

Lima beans contain linamarin, a cyanogenic glucoside, although the beans are rendered safe when cooked, and low-linamarin varieties are typically used for culinary purposes. Cyanogenic glycosides are present in green plant tissue as well as in seeds such as Almonds, flax seed, and wild Lima beans (5).


Early studies demonstrated that Lima bean contains at least 23 proteins that may have allergenic potential (6).

In a survey of food allergy among asthma and rhinitis patients in Delhi, India, evaluation of sera of patients with evidence of Lima bean skin reactivity demonstrated 12 IgE binding proteins of 18-96 kDa in Lima bean (7-8).

More recently, a study examining the in vitro cross-reactivity of Mesquite pollen and Lima bean demonstrated the presence of 20, 26, 35, 66 and 72 kDa proteins as shared IgE binding components between the 2 extracts (8).

Other proteins of unknown allergenic potential have previously been isolated; they have been shown to have allergenic potential in other plants. These include a 20 kDa cysteine proteinase inhibitor with an N-terminal sequence homologous to other members of the cystatins. The protein was relatively heat-labile, which suggested it could be inactivated with normal cooking (9). A trypsin inhibitor was isolated (10) and shown to be very thermostable, retaining activity even after boiling for 10 minutes (11).

Potential cross-reactivity

There are reports suggesting, based on SPT, that Lima bean cross-reacts with other allergenic legumes, such as Soya, Peanut, and black gram (6,12-13).

However, previous studies have demonstrated that, although the degree of biochemical cross-reactivity among members of the legume family is high, the clinical significance of this is low, so that being allergic to one legume does not necessarily require excluding other legumes from the diet. Results of skin prick tests alone should not be used for prescribing prolonged food restriction diets (12).

This is also suggested by a study reporting that only 2 of 41 legume-allergic patients (diagnosed by double-blind, placebo-controlled oral food challenge or "convincing history" of anaphylaxis) had an IgE-mediated hypersensitivity reaction to more than a single member of the legume family, even though extensive immunologic cross-reactivity was demonstrated among legume antigens in in vitro and in vivo assessments of 6 legumes (Peanut, Soybean, Lima bean, Pea, garbanzo bean and Green beans) (6).

The particular allergen within a legume will probably determine the extent and degree of cross-reactivity. This is illustrated by a report of a patient who suffered adverse reactions when eating Peas, Lentils, Peanuts, Kidney, Lima and navy beans; he experienced the most severe episodes following ingestion of Soybean products. A IgE antibody response to the Kunitz Soybean trypsin inhibitor polypeptide was demonstrated (14).

IgE-mediated food allergy often develops as a consequence of allergic sensitisation to pollen proteins. Recently, cross-reactivity was demonstrated between Mesquite tree pollen (Prosopis juliflora) and Lima bean as a food, both members of the family Leguminosae (Fabaceae).

In a study of 110 patients with asthma and/or rhinitis, of whom 20 showed marked positive reactions with Prosopis pollen extract, 12 patients showed elevated IgE antibody level to Prosopis pollen extract alone and 4 to both Phaseolus and pollen extract. P. lunatus extract could inhibit IgE binding to P. juliflora in a dose-dependent manner. The presence of 20, 26, 35, 66 and 72 kDa proteins as shared IgE binding components between the 2 extracts was demonstrated (8).

A study reported on a 33-year-old woman who developed tongue swelling and burning and mouth itching within minutes of eating baked beans. Similar symptoms occurred following ingestion of other legume products, including Peas, a bean burrito, and Kidney and pinto beans. SPT was positive to Red kidney and White beans but not to Pea, string or Lima beans, confirming that cross-reactivity between the legumes is not absolute (15).

Clinical Experience

IgE-mediated reactions

Lima bean may induce symptoms of food allergy in sensitised individuals, although this is uncommon (12-13).

However, a number of studies have demonstrated sensitisation to Lima bean. In a survey of food allergy among asthma and rhinitis patients in Delhi, India, when allergy to Lima bean was claimed on history, sensitisation to Lima bean using SPT was demonstrated in approximate 3-4% (16) of 470 cases. Immunoblot analysis with allergic patients' sera confirmed and demonstrated the presence of IgE binding proteins in Lima bean (7).

In a study that investigated the in vitro cross-reactivity of Mesquite pollen and Lima bean, of 110 patients with asthma, rhinitis or both, 20 were shown to have IgE antibodies to Mesquite pollen extract; and of these, 12 patients showed elevated IgE antibody level to Mesquite pollen extract alone, and 4 to both Lima bean and pollen extract (8).


  1. Adeparusi EO. Effect of processing on the nutrients and anti-nutrients of lima bean (Phaseolus lunatus L.) flour.
    Nahrung 2001;45(2):94-6
  2. Wikipedia. Phaseolus lunatus.
    Accessed May 2008
  3. Sparvoli F, Lanave C, Santucci A, Bollini R, Lioi L. Lectin and lectin-related proteins in lima bean (Phaseolus lunatus L.) seeds: biochemical and evolutionary studies.
    Plant Mol Biol 2001;45(5):587-97
  4. Feria M, Pérez-Santiago A, Cuevas D, Martínez M, Córdoba F. Purification and partial characterization of a new anti-A1 lectin of Phaseolus coccineus collected in Oaxaca, Mexico.
    Prep Biochem Biotechnol 1996;26(1):31-46
  5. Frehner M, Scalet M, Conn EE. Pattern of the Cyanide-Potential in Developing Fruits : Implications for Plants Accumulating Cyanogenic Monoglucosides (Phaseolus lunatus) or Cyanogenic Diglucosides in Their Seeds (Linum usitatissimum, Prunus amygdalus). Plant Physiol 1990;94(1):28-34
  6. Bernhisel Broadbent J, Taylor S, Sampson HA. Cross-allergenicity in the legume botanical family in children with food hypersensitivity. II. Laboratory correlates. J Allergy Clin Immunol 1989;84(5 Pt 1):701-9
  7. Indian Council of Medical Research Studies on foods as sensitizing and inducing factors of allergy disorders with special reference to bronchial asthma. Project report: New Delhi: Indian Council of Medical Research Indian Council of Medical Research 2006:1-34
  8. Dhyani A, Arora N, Jain VK, Sridhara S, Singh BP. Immunoglobulin E (IgE)-mediated cross-reactivity between mesquite pollen proteins and lima bean, an edible legume. Clin Exp Immunol 2007;149(3):517-24
  9. Lawrence JC, Nielsen SS. Partial isolation and characterization of a cysteine proteinase inhibitor from Lima bean (Phaseolus lunatus).
    J Agric Food Chem 2001;49(2):1020-5
  10. Birk Y. Lima bean trypsin inhibitors.
    Methods Enzymol 1976;45:707-9
  11. Samudzi C, Schroeder S, Griffith S, Chen X, Quinn TP. Crystallization and preliminary studies of lima bean trypsin inhibitor. Proteins 1997;27(2):311-4
  12. Bernhisel Broadbent J, Sampson HA. Cross-allergenicity in the legume botanical family in children with food hypersensitivity.
    J Allergy Clin Immunol 1989;83:435-40
  13. Kumar R, Singh BP, Srivastava P, Sridhara S, Arora N, Gaur SN. Relevance of serum IgE estimation in allergic bronchial asthma with special reference to food allergy. Asian Pac J Allergy Immunol 2006;24(4):191-9
  14. Moroz LA, Yang WH. Kunitz soybean trypsin inhibitor: a specific allergen in food anaphylaxis.
    N Engl J Med 1980;302(20):1126-8
  15. Zacharisen MC, Kurup V. Anaphylaxis to beans. J Allergy Clin Immunol 1998;101(4 Pt 1):556-7

As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.