Advertisement

Plant Proteins from Legumes

  • Catherine Bennetau-Pelissero
Living reference work entry
Part of the Reference Series in Phytochemistry book series (RSP)

Abstract

Legumes are part of the human edible panel since prehistory times but the remains that reached our last centuries were all from a period posterior to fire domestication. In all parts of the world where human civilizations developed, pulses were associated with cereals and the combination of their proteins managed to cover the essential amino-acid requirements of Humans and animals. Legumes gathering more than 19,000 different species, all present high protein content due to specific symbiosis with rhizobia and arbuscular mycorrhizae present in the soils. These associations are thought to originate from first symbiotic events dating from more than 60 million years before present. They allow the plants to fix nitrogen that is used for protein biosynthesis. The nutritional value of actual pulses is generally higher than that of other crops especially since domestication and the genetic selection processes operated by humans. Beside proteins with suitable amino-acid profiles, legumes also contain digestible carbohydrates and some of them also contain fat. In some cases, these fat include polyunsaturated fatty acids that increase further the nutritional value of the corresponding legumes. However, if such valuable plants managed to survive along geological periods, it is because their evolution with their environmental pressure lead them to develop anti-nutritional substances to protect themselves from their predators. Here will be discussed some of these anti-nutritional substances, the so-called tannins, phytic acid, saponins, phytoestrogens, lipoxygenase, hemagglutinin, trypsin inhibitor, as well as allergens. Because all these substances are basically useful for the crops, it is only during processing that they should be removed. Therefore, a special focus is made on traditional versus modern recipes and industrial food processing. Their respective impacts on basic nutritional components (amino-acids, fats, carbohydrates, vitamins, and minerals) as well as on the anti-nutritional factors listed above are examined. Basically, wet processing which was most frequently developed in the past, associated orf not with fermentation or germination, is also the most efficient in removing all anti-nutritional factors.

Keywords

Legumes Prehistoric domestication Proteins Amino-acid profiles Anti-nutritional factors Tannins Saponins Phytic Acids Phytoestrogens Oligosaccharids Hemagglutinins Lipoxygenases Tripsin inhibitors Allergens 

References

  1. 1.
    Caracuta V, Barzilai O, Khalaily H, Milevski I, Paz Y, Vardi J, Regev L, Boaretto E (2015) The onset of faba bean farming in the Southern Levant. Sci Rep 5:14370–14379PubMedPubMedCentralCrossRefGoogle Scholar
  2. 2.
    Abbo S (2011) Experimental growing of wild pea in Israel and its bearing on Near Eastern plant domestication. Ann Bot 107:1399–1404PubMedPubMedCentralCrossRefGoogle Scholar
  3. 3.
    Ladizinsky G (1993) Lentil domestication: on the quality of evidence and arguments. Econ Bot 47:60–64 (17, 18, 20)CrossRefGoogle Scholar
  4. 4.
    Kerem Z, Lev-Yadun S, Gopher A, Weinberg P, Abbo S (2007) Chickpea domestication in the Neolithic Levant through the nutritional perspective. J Archaeol Sci 34:1289–1293CrossRefGoogle Scholar
  5. 5.
    Werker E, Marbach I, Mayer AM (1979) Relation between the anatomy of the testa, water permeability and the presence of phenolics in the genus Pisum. Ann Bot 43:765–771CrossRefGoogle Scholar
  6. 6.
    Butler A (1989) In: Harris DR, Hillman GC (eds) Foraging and farming. Unwin and Hayman, London, pp 390–407Google Scholar
  7. 7.
    Hillman GC, Wales S, McClaren F, Evans J, Butler A (1993) Identifying problematic remains of ancient plant foods: a comparison of the role of chemical, histological and morphological criteria. World Archaeol 25:94–121PubMedCrossRefPubMedCentralGoogle Scholar
  8. 8.
    Zohary D, Hopf M (1973) Domestication of pulses in the old world. Legumes were companions of wheat and barley when agriculture began in the Near East. Science 182:887–894PubMedCrossRefPubMedCentralGoogle Scholar
  9. 9.
    van Zeist W, Bottema S (1966) Palaeobotanical investigation at Ramad. Ann Archeol Arabes Syr 16:179–180Google Scholar
  10. 10.
    Helbaek H (1964) First impressions of the Çatal Hüyük plant husbandry. Anatol Stud 14:121–123CrossRefGoogle Scholar
  11. 11.
    Helbaek H (1969) Plant collecting, dry-farming and irrigation agriculture in prehistoric Deh Luran. In: Hole F, ICV F, Neely JA (eds) Prehistory and human ecology of the Deh Luran Plain. Memoirs of the museum of anthropology, no 1. University of Michigan, Ann Arbor, pp 383–426Google Scholar
  12. 12.
    Helbaek H (1970) In: Mellaart J (ed) Excavations at Hacilar. Edinburgh University Press, Edinburgh, p 189Google Scholar
  13. 13.
    Garrard A (1999) Charting the emergence of cereal and pulse domestication in Southwest Asia. Environ Archaeol 4:67–86CrossRefGoogle Scholar
  14. 14.
    Abbo S, Shtienberg D, Lichtenzveig J, Lev-Yadun S, Gopher A (2003) The chickpea, summer cropping, and a new model for pulse domestication in the ancient near east. Q Rev Biol 78(4):37–50CrossRefGoogle Scholar
  15. 15.
    Cubero JI (1974) On the evolution of Vicia faba L. Theor Appl Genet 45:47–51PubMedCrossRefPubMedCentralGoogle Scholar
  16. 16.
    Gaut BS (2014) The complex domestication history of the common bean. Nat Genet 46(7):663–664PubMedCrossRefPubMedCentralGoogle Scholar
  17. 17.
    Bitocchi E, Bellucci E, Giardini A, Rau D, Rodriguez M, Biagetti E, Santilocchi R, Spagnoletti Zeuli P, Gioia T, Logozzo G, Attene G, Nanni L, Papa R (2013) Molecular analysis of the parallel domestication of the common bean (Phaseolus vulgaris) in Mesoamerica and the Andes. New Phytol 197:300–313PubMedCrossRefPubMedCentralGoogle Scholar
  18. 18.
    Beebe S, Skroch PW, Tohme J, Duque MC, Pedraza F, Nienhuis J (2000) Structure of genetic diversity among common bean landraces of Middle American origin based on correspondence analysis of RAPD. Crop Sci 40:264–273CrossRefGoogle Scholar
  19. 19.
    Singh SP, Gepts P, Debouck DG (1991) Races of common bean (Phaseolus vulgaris, Fabaceae). Econ Bot 45:379–396CrossRefGoogle Scholar
  20. 20.
    Gepts P, Kmiecik K, Pereira P, Bliss FA (1988) Dissemination pathways of common bean (Phaseolus vulgaris, Fabaceae) deduced from phaseolin electrophoretic variability. I. The Americas. Econ Bot 42:73–85CrossRefGoogle Scholar
  21. 21.
    Papa R, Gepts P (2003) Asymmetry of gene flow and differential geographical structure of molecular diversity in wild and domesticated common bean (Phaseolus vulgaris L.) from Mesoamerica. Theor Appl Genet 106:239–250PubMedCrossRefPubMedCentralGoogle Scholar
  22. 22.
    Atchison GW, Nevado B, Eastwood RJ, Contreras-Ortiz N, Reynel C, Madriñán S, Filatov DA, Hughes CE (2016) Lost crops of the Incas: origins of domestication of the Andean pulse crop ‘tarwi’ Lupineus mutabilis. Am J Bot 103(9):1592–1606PubMedCrossRefPubMedCentralGoogle Scholar
  23. 23.
    Bonavia D (1982) Preceramico Peruano. Los Gavilanes. Mar, Desierto y Oasis en La Historia del Hombre. Corporacio’n Financiera de Desarrollo S.A. COFIDE and Instituto Arqueologico Aleman, LimaGoogle Scholar
  24. 24.
    Krapovickas A, Gregory WC (1994) Taxonomıa del genero Arachis (Leguminosae). Bonplandia 8:1–186Google Scholar
  25. 25.
    Grabiele M, Chalup A, German Robledo G, Seijo G (2015) Genetic and geographic origin of domesticated peanut as evidenced by 5S rDNA and chloroplast DNA sequences. Plant Syst Evol 298:1151–1165CrossRefGoogle Scholar
  26. 26.
    Smartt J (1990) Grain legumes: evolution and genetic resources. Cambridge University Press, Cambridge, pp 140–175CrossRefGoogle Scholar
  27. 27.
    Kongjaimun A, Kaga A, Tomooka N, Somta P, Vaughan DA, Srinives P (2012) The genetics of domestication of yardlong bean, Vigna unguiculata (L.) Walp. ssp. unguiculata cv.-gr. sesquipedalis. Ann Bot 109:1185–1200PubMedPubMedCentralCrossRefGoogle Scholar
  28. 28.
    D’Andrea AC, Kahlheber S, Logan X, Watson DJ (2007) Early domesticated cowpea (Vigna unguiculata) from Central Ghana. Antiquity 81:686–698CrossRefGoogle Scholar
  29. 29.
    D’Andrea AC, Logan AL, Watson DJ (2006) Oil palm and prehistoric subsistence in tropical West Africa. J Afr Archaeol 4(2):195–222CrossRefGoogle Scholar
  30. 30.
    Coulibaly S, Pasquet RS, Papa R, Gepts P (2002) AFLP analysis of the phenetic organization and genetic diversity of Vigna unguiculata L. Walp. Reveals extensive gene flow between wild and domesticated types. Theor Appl Genet 104(2–3):358–366PubMedCrossRefPubMedCentralGoogle Scholar
  31. 31.
    Lambot C (2002) Industrial potential of cowpea. In: Fatokun CA, Tarawali SA, Singh PM, Kormawa PM, Tarmo M (eds) Challenges and opportunities for enhancing sustainable cowpea production. International Institute of Tropical Agriculture, Ibadan, pp 367–375Google Scholar
  32. 32.
    Basu S, Mayes S, Davey M, Roberts JA, Azam-Ali SN, Mithen R, Pasquet RS (2007) Inheritance of ‘domestication’ traits in bambara groundnut (Vigna subterranea (L.) Verdc.). Euphytica 157:59–68CrossRefGoogle Scholar
  33. 33.
    Philippson G, Serge Bahuchet S (1994) Cultivated crops and bantu migrations in central and eastern Africa: a linguistic approach. Archaeol Res Afr 29–30(1):103–120Google Scholar
  34. 34.
    Frahm-Leliveld JA (1953) Some chromosome numbers in tropical leguminous plants. Euphytica 2:46–48Google Scholar
  35. 35.
    Deng Z, Qin L, Gao Y, Weisskopf AR, Zhang C, Fuller DCQ (2015) From early domesticated rice of the middle Yangtze Basin to millet, rice and wheat agriculture: archaeobotanical macro-remains from Baligang, Nanyang Basin, Central China (6700–500 BC). PLoS One 10(10):e0139885PubMedPubMedCentralCrossRefGoogle Scholar
  36. 36.
    Hymowitz T (1970) On the domestication of the soybean. Econ Bot 24:408–421CrossRefGoogle Scholar
  37. 37.
    Fehr WR (1980) Soybean. In: Ferh W, Hadley HH (eds) Hybridization of crop plants. American Society of Agronomy, Madison, pp 589–599Google Scholar
  38. 38.
    Canadian Food Inspection Agency (1996) The biology of Glycine max (L.) Merr. (Soybean) Biology Document BIO1996–10; 11pGoogle Scholar
  39. 39.
    Willis H (1989) Growing great soybeans. Acres USA 1, 6–8Google Scholar
  40. 40.
    Shurtleff W, Huang HT, Aoyagi A (2014) History of soybeans and soyfoods in China and Taiwan, and in chinese cookbooks, restaurants, and Chinese work with soyfoods Outside china Including Manchuria, Hong Kong and Tibet (1024 BCE to 2014). Soyinfo Center, Lafayette 3015pGoogle Scholar
  41. 41.
    Sprent JI (2008) 60 Ma of legume nodulation. What’s new? What’s changing? J Exp Bot 59:1081–1084PubMedCrossRefPubMedCentralGoogle Scholar
  42. 42.
    Doyle JJ (2011) Phylogenetic perspectives on the origins of nodulation. Mol Plant-Microbe Interact 24:1289–1295PubMedCrossRefPubMedCentralGoogle Scholar
  43. 43.
    Sprent JI (2007) Evolving ideas of legume evolution and diversity: a taxonomic perspective on the occurrence of nodulation. New Phytol 174:11–25PubMedCrossRefPubMedCentralGoogle Scholar
  44. 44.
    Ivanov S, Fedorova EE, Limpens E, De Mita S, Genre A, Bonfante P, Bisseling T (2012) Rhizobium-legume symbiosis shares exocytotic pathway required for arbuscule formation. PNAS USA 109:8316–8321PubMedCrossRefPubMedCentralGoogle Scholar
  45. 45.
    Mierziak J, Kostyn K, Kulma A (2014) Flavonoids as important molecules of plant interactions with the environment. Molecules 19:16240–16265PubMedCrossRefPubMedCentralGoogle Scholar
  46. 46.
    Pueppke SG (1996) The genetic and biochemical basis for nodulation of legumes by rhizobia. Crit Rev Biotechnol 16:1–51PubMedCrossRefPubMedCentralGoogle Scholar
  47. 47.
    Desbrosses GJ, Stougaard J (2011) Root nodulation: a paradigm for how plant-microbe symbiosis influences host developmental pathways. Cell Host Microbe 10(4):348–358PubMedCrossRefPubMedCentralGoogle Scholar
  48. 48.
    Peters NK, Frost JW, Long SR (1986) A plant flavone, luteolin, induces expression of Rhizobium meliloti nodulation genes. Science 233(4767):977–980PubMedCrossRefPubMedCentralGoogle Scholar
  49. 49.
    Hartwig UA, Maxwell CA, Joseph CM, Phillips DA (1990) Chrysoeriol and luteolin released from alfalfa seeds induce nod genes in Rhizobium meliloti. Plant Physiol 92:116–122PubMedPubMedCentralCrossRefGoogle Scholar
  50. 50.
    Kuzma MM, Hunt S, Layzell DB (1993) Role of oxygen in the limitation and inhibition of nitrogenase activity and respiration rate in individual soybean nodules. Plant Physiol 101:161–169PubMedPubMedCentralCrossRefGoogle Scholar
  51. 51.
    Ott T, van Dongen JT, Gunther C, Krusell L, Desbrosses G et al (2005) Symbiotic leghemoglobins are crucial for nitrogen fixation in legume root nodules but not for general plant growth and development. Curr Biol 15:531–535PubMedCrossRefPubMedCentralGoogle Scholar
  52. 52.
    Udvardi M, Poole PS (2013) Transport and metabolism in legume-rhizobia symbioses. Annu Rev Plant Biol 64:781–805PubMedCrossRefPubMedCentralGoogle Scholar
  53. 53.
    Vance CP, Gantt JS (1992) Control of nitrogen and carbon metabolism in root-nodules. Physiol Plant 85:266–274CrossRefGoogle Scholar
  54. 54.
    Pate JS, Atkins CA, White ST, Rainbird RM, Woo KC (1980) Nitrogen nutrition and xylem transport of nitrogen in ureide producing grain legumes. Plant Physiol 65:961–965PubMedPubMedCentralCrossRefGoogle Scholar
  55. 55.
    Heath KD, McGhee KE (2012) Coevolutionary constraints? The environment alters tripartite interaction traits in a legume. PLoS One 7(7):e41567PubMedPubMedCentralCrossRefGoogle Scholar
  56. 56.
    Martínez-Romero E (2009) Coevolution in rhizobium-legume symbiosis? DNA Cell Biol 28(8):361–370PubMedCrossRefPubMedCentralGoogle Scholar
  57. 57.
    Andam CP, Parker MA (2008) Origins of Bradyrhizobium nodule symbionts from two legume trees in the Philippines. J Biogeogr 35:1030–1039CrossRefGoogle Scholar
  58. 58.
    Maillet F, Poinsot V, Andre O, Puech-Pages V, Haouy A, Gueunier M, Cromer L, Giraudet D, Formey D, Niebel A (2011) Fungal lipochitooligosaccharide symbiotic signals in arbuscular mycorrhiza. Nature 469:58–64PubMedCrossRefPubMedCentralGoogle Scholar
  59. 59.
    Smit P, Limpens E, Geurts R, Fedorova E, Dolgikh E, Gough C, Bisseling T (2007) Medicago L YK3, an entry receptor in rhizobial nodulation factor signaling1[W]. Plant Physiol 145:183–191PubMedPubMedCentralCrossRefGoogle Scholar
  60. 60.
    Pietraszewska-Bogiel A, Lefebvre B, Koini MA, Klaus-Heisen D, Takken FLW, Geurts R, Cullimore JV, Gadell TWJ (2013) Interaction of Medicago truncatula lysin motif receptor-like kinases, NFP and LYK3, produced in Nicotiana benthamiana induces defence-like responses. PLoS One 8:e65055PubMedPubMedCentralCrossRefGoogle Scholar
  61. 61.
    Rubio LA, Pérez A, Ruiz R, Guzmán MÁ, Aranda-Olmedo I, Clemente A (2014) Characterization of pea (Pisum sativum) seed protein fractions. J Sci Food Agric 94(2):280–287PubMedCrossRefPubMedCentralGoogle Scholar
  62. 62.
    Yaklich RW (2001) β-Conglycinin and glycinin in high-protein soybean seeds. J Agric Food Chem 49:729–735PubMedCrossRefPubMedCentralGoogle Scholar
  63. 63.
    Cabello-Hurtado F, Keller J, Ley J, Sanchez-Lucas R, Jorrín-Novo JV, Aïnouche A (2016) Proteomics for exploiting diversity of lupine seed storage proteins and their use as nutraceuticals for health and welfare. J Proteome 143:57–68CrossRefGoogle Scholar
  64. 64.
    Duranti M, Restani P, Poniatowska M, Cerletti P (1981) The seed globulins of Lupineus albus. Phytochemistry 20:2071–2075CrossRefGoogle Scholar
  65. 65.
    Barać M, Cabrilo S, Pešić M, Stanojević S, Pavlićević M, Maćej O, Ristić N (2011) Functional properties of pea (Pisum sativum, L.) protein isolates modified with chymosin. Int J Mol Sci 12(12):8372–8387PubMedPubMedCentralCrossRefGoogle Scholar
  66. 66.
    De Pace C, Delre V, Scarascia Mugnozza GT, Maggini F, Cremonini R, Frediani M, Cionini PG (1991) Legumin of Vicia faba major: accumulation in developing cotyledons, purification, mRNA characterization and chromosomal location of coding genes. Theor Appl Genet 83(1):17–23PubMedCrossRefPubMedCentralGoogle Scholar
  67. 67.
    Derbyshire E, Wright DJ, Boulter D (1976) Legumin and vicilin, storage proteins of legume seeds. Phytochemistry I5:3–24CrossRefGoogle Scholar
  68. 68.
    Pusztai A, Stewart JC (1980) Molecular size, subunit structure and microhet§of glycoprotein II from the seeds of kidney bean (Phaseolus vulgaris L.). Biochim Biophys Acta 623(2):418–428PubMedCrossRefPubMedCentralGoogle Scholar
  69. 69.
    Carbonaro M, Grant G, Cappelloni M, Pusztai A (2000) Perspectives into factors limiting in vivoèjn4 digestion of legume proteins: antinutritional compounds or storage proteins? J Agric Food Chem 48(3):742–749PubMedCrossRefPubMedCentralGoogle Scholar
  70. 70.
    Bouchenak M, Lamri-Senhadji M (2013) Nutritional quality of legumes, and their role in cardiometabolic risk prevention: a review. J Med Food 16(3):185–198PubMedCrossRefPubMedCentralGoogle Scholar
  71. 71.
    Nosworthy MG, Medina G, Franczyk AJ, Neufeld J, Appah P, Utioh A, Frohlich P, House JD (2018) Effect of processing on the in vitro and in vivo protein quality of red and green lentils (Lens culinaris). Food Chem 240:588–593PubMedCrossRefPubMedCentralGoogle Scholar
  72. 72.
    Tömösközi S, Lásztity R, Haraszi R, Baticz O (2001) Isolation and study of the functional properties of pea proteins. Nahrung 45(6):399–401PubMedCrossRefPubMedCentralGoogle Scholar
  73. 73.
    Rachwa-Rosiak D, Nebesny E, Budryn G (2015) Chickpeas – composition, nutritional value, health benefits, application to bread and snacks: a review. Crit Rev Food Sci Nutr 55(8):1137–1145PubMedCrossRefPubMedCentralGoogle Scholar
  74. 74.
    Lizarazo CI, Lampi AM, Liu J, Sontag-Strohm T, Piironen V, Stoddard FL (2017) Nutritive quality and protein production from grain legumes in a boreal climate. J Sci Food Agric 97(6):2053–2064CrossRefGoogle Scholar
  75. 75.
    Nosworthy MG, Franczyk A, Zimoch-Korzycka A, Appah P, Utioh A, Neufeld J, House JD (2017) Impact of processing on the protein quality of pinto bean (Phaseolus vulgaris) and buckwheat (Fagopyrum esculentum Moench) flours and blends, as determined by in vitro and in vivo methodologies. J Agric Food Chem 65(19):3919–3925PubMedCrossRefPubMedCentralGoogle Scholar
  76. 76.
    Prathiba KM, Reddy MU (1994) Nutrient composition of groundnut cultures (Arachis hypogaea L.) in relation to their kernel size. Plant Foods Hum Nutr 45(4):365–369PubMedCrossRefPubMedCentralGoogle Scholar
  77. 77.
    Hussain MA, Basahy AY (1998) Nutrient composition and amino acid pattern of cowpea (Vigna unguiculata (L.) Walp, Fabaceae) grown in the Gizan area of Saudi Arabia. Int J Food Sci Nutr 49(2):117–124PubMedCrossRefPubMedCentralGoogle Scholar
  78. 78.
    Yao DN, Kouassi KN, Erba D, Scazzina F, Pellegrini N, Casiraghi MC (2015) Nutritive evaluation of the Bambara groundnut Ci12 landrace [Vigna subterranea (L.) Verdc. (Fabaceae)] produced in Côte d’Ivoire. Int J Mol Sci 16(9):21428–21441PubMedCrossRefPubMedCentralGoogle Scholar
  79. 79.
    Mubarak AE (2005) Nutritional composition and antinutritional factors of mung bean seeds (Phaseolus aureus) as affected by some home traditional processes. Food Chem 89:489–495CrossRefGoogle Scholar
  80. 80.
    Kouris-Blazos A, Belski R (2016) Health benefits of legumes and pulses with a focus on Australian sweet lupines. Asia Pac J Clin Nutr 21(1):1–17Google Scholar
  81. 81.
    Staniak M, Księżak J, Bojarszczuk J (2014) Chapter 6: Mixtures of legumes with cereals as a source of feed for animals. In: Organic agriculture towards sustainability. Tech Open Publisher, pp 123–145.  https://doi.org/10.5772/58358Google Scholar
  82. 82.
    Maphosa Y, Jideani VA (2017) Chapter 6: The role of legumes in human nutrition. In: Functional food – improve health through adequate food. Intechopen Publisher, pp 103–121.  https://doi.org/10.5772/intechopen.69127Google Scholar
  83. 83.
    Gupta YP (1987) Anti-nutritional and toxic factors in food legumes: a review. Plant Foods Hum Nutr 37(3):201–228PubMedCrossRefPubMedCentralGoogle Scholar
  84. 84.
    Bate-Smith EC, Swain T (1962) Flavonoid compounds. In: Mason HS, Florkin AM (eds) Comparative biochemistry. Academic, New York, pp 755–809Google Scholar
  85. 85.
    Jansman AJM, Longstaff M (1993) Nutritional effects of tannins and vicine/covicine in legume seeds. In: van der Poel AFB, Huisman J, Saini HS (eds) Proceedings of the second international workshop on “Antinutritional factors (ANFS) in legume seeds”. Pers Wageningen, Wageningen, pp 301–316Google Scholar
  86. 86.
    Shimelis EA, Rakshit SK (2007) Effect of processing on antinutrients and in vitro protein digestibility of kidney bean (Phaseolus vulgaris L.) varieties grown in East Africa. Food Chem 103:161–172CrossRefGoogle Scholar
  87. 87.
    Zia-ur-Rehman, Shah WH (2001) Tannin contents and protein digestibility of black grams (Vigna mungo) after soaking and cooking. Plant Food Hum Nutr 56:265–273CrossRefGoogle Scholar
  88. 88.
    Duodu KG, Taylor JRN, Belton PS, Hamakerc BR (2003) Factors affecting sorghum protein digestibility. J Cereal Sci 38:117–131CrossRefGoogle Scholar
  89. 89.
    Elkin RG, Freed MB, Hamaker BR, Zhang Y, Parsons CM (1996) Condensed tannins are only partially responsible for variations in nutrient digestibilities of sorghum grain cultivars. J Agric Food Chem 44:848–853CrossRefGoogle Scholar
  90. 90.
    Jansman AFJ, Frohlich AA, Marquardt RR (1994) Production of proline-rich proteins by the parotid glands of rats is enhanced by feeding diets containing tannins from faba beans (Vicia faba L.). J Nutr 124:249–258PubMedCrossRefPubMedCentralGoogle Scholar
  91. 91.
    Mehansho H, Asquith TN, Butler LG, Rogler JC, Carlson DM (1992) Tannin mediated induction of proline-rich protein synthesis. J Agric Food Chem 40:93–97CrossRefGoogle Scholar
  92. 92.
    Gilani GS, Xiao CW, Cockell KA (2012) Impact of Antinutritional Factors in Food Proteins on the Digestibility of Protein and the Bioavailability of Amino Acids and on Protein Quality. Brit J Nutr 108:S315–S332CrossRefGoogle Scholar
  93. 93.
    Harland BF, Oberleas D (1987) Phytates in foods. World Rev Nutr Diet 52:235–259PubMedCrossRefPubMedCentralGoogle Scholar
  94. 94.
    Chitra U, Vimala V, Singh U, Geervani P (1995) Variability in phytic acid content and protein digestibility of grain legumes. Plant Foods Hum Nutr 47:163–172PubMedCrossRefPubMedCentralGoogle Scholar
  95. 95.
    Batista KA, Prudencio SH, Fernandes KE (2010) Changes in functional properties and antinutritional factors of extruded hard-to-cook common beans (Phaseolus vulgaris L.). J Food Sci 75:C286–C290PubMedCrossRefPubMedCentralGoogle Scholar
  96. 96.
    Vaintraub IA, Bulmaga VP (1991) Effect of phytate on the in vitro activity of digestive proteinases. J Agric Food Chem 39:859–861CrossRefGoogle Scholar
  97. 97.
    Lothia D, Hoch H, Kievernagel Y (1987) Influence of phytate on in vitro digestibility of casein under physiological conditions. Plant Foods Hum Nutr 37:229–235CrossRefGoogle Scholar
  98. 98.
    Ravindran V, Cabahug S, Ravindran G, Bryden WL (1999) Influence of microbial phytase on apparent ileal amino acid digestibility of food stuffs for broilers. Poult Sci 78:699–706PubMedCrossRefPubMedCentralGoogle Scholar
  99. 99.
    Selle PH, Ravindran V, Caldwell RA, Bryden WL (2000) Phytate and phytase; consequences for protein utilisation. Nutr Res Rev 13:255–278PubMedCrossRefPubMedCentralGoogle Scholar
  100. 100.
    Gulewicz P, Ciesiołka D, Frias J, Vidal-Valverde C, Frejnagel S, Trojanowska K, Gulewicz K (2000) Simple method of isolation and purification of alpha-galactosides from legumes. J Agric Food Chem 48(8):3120–3123PubMedCrossRefPubMedCentralGoogle Scholar
  101. 101.
    Fan P-H, Zang M-T, Xing J (2015) Oligosaccharides composition in eight food legumes species as detected by high-resolution mass spectrometry. J Sci Food Agric 95:2228–2236PubMedCrossRefPubMedCentralGoogle Scholar
  102. 102.
    Gangola MP, Jaiswal S, Khedikar YP, Chibbar RN (2014) A reliable and rapid method for soluble sugars and RFO analysis in chickpea using HPAEC-PAD and its comparison with HPLC-RI. Food Chem 154:127–133PubMedCrossRefPubMedCentralGoogle Scholar
  103. 103.
    Cerning-Béroard J, Filiatre-Verel A (1980) Characterization and distribution of soluble and insoluble carbohydrates in lupine seeds. Z Lebensm Unters Forsch 171(4):281–285PubMedCrossRefPubMedCentralGoogle Scholar
  104. 104.
    Tharanathan RN, Wankhede DB, Rao M, Rao RR (1975) Carbohydrate composition of groundnuts (Arachis hypogea). J Sci Food Agric 26(6):749–754PubMedCrossRefPubMedCentralGoogle Scholar
  105. 105.
    Adeleke OR, Adiamo OQ, Fawale OS, Olamiti G (2017) Effect of soaking and boiling on Antinutritional factors, oligosaccharide contents and protein digestibility of newly developed Bambara groundnut cultivars Turk. J Agric Food Sci Technol 5(9):1006–1014Google Scholar
  106. 106.
    Devindra S, Rao SJ, Krishnaswamy P, Bhaskar V (2011) Reduction of α-galactoside content in red gram (Cajanus cajan L.) upon germination followed by heat treatment. J Sci Food Agric 91(10):1829–1835PubMedCrossRefPubMedCentralGoogle Scholar
  107. 107.
    Olson AC, Gray GM, Grambmann MR, Wagner IR (1981) Flatus causing factors in legumes. In: Ory RL (ed) Antinutrients and natural toxicants in food. Food and Nutritional Press, Westport, pp 275–294Google Scholar
  108. 108.
    Liener IE (1994) Implications of antinutritional components in soybean food. Crit Rev Food Sci Nutr 34:31–37PubMedCrossRefPubMedCentralGoogle Scholar
  109. 109.
    De Hoff PL, Brill LM, Hirsch AM (2009) Plant lectins: the ties that bind in root symbiosis and plant defense. Mol Gen Genomics 282(1):1–15CrossRefGoogle Scholar
  110. 110.
    He S, Simpson BK, Sun H, Ngadi MO, Ma Y, Huang T (2018) Phaseolus vulgaris lectins: a systematic review of characteristics and health implications. Crit Rev Food Sci Nutr 58(1):70–83PubMedCrossRefPubMedCentralGoogle Scholar
  111. 111.
    Loris R, Hamelryck T, Bouckaert J, Wyns L (1998) Legume lectin structure. BBA-Protein Struct M 1383(1):9–36CrossRefGoogle Scholar
  112. 112.
    Kumar S, Sharma A, Das M, Jain SK, Dwivedi PD (2014) Leucoagglutinating phytohemagglutinin: purification, characterization, proteolytic digestion and assessment for allergenicity potential in BALB/c mice. Immunopharmacol Immunotoxicol 36(2):138–144PubMedCrossRefPubMedCentralGoogle Scholar
  113. 113.
    Hirabayashi J, Kuno A, Tateno H (2011) Lectin-based structural glycomics: a practical approach to complex glycans. Electrophoresis 32(10):1118–1128PubMedCrossRefPubMedCentralGoogle Scholar
  114. 114.
    Gabius H-J, André S, Jiménez-Barbero J, Romero A, Solís D (2011) From lectin structure to functional glycomics: principles of the sugar code. Trends Biochem Sci 36(6):298–313PubMedCrossRefPubMedCentralGoogle Scholar
  115. 115.
    Brewer CF, Brown Iii RD, Koenig SH (1983) Metal ion binding and conformational transitions in concanavalin A: a structure-function study. J Biomol Struct Dyn 1(4):961–997PubMedCrossRefPubMedCentralGoogle Scholar
  116. 116.
    Menard S, Cerf-Bensussan N, Heyman M (2010) Multiple facets of intestinal permeability and epithelial handling of dietary antigens. Mucosal Immunol 3(3):247–259PubMedCrossRefPubMedCentralGoogle Scholar
  117. 117.
    Bardocz S, Grant G, Ewen S, Duguid T, Brown D, Englyst K, Pusztai A (1995) Reversible effect of phytohaemagglutinin on the growth and metabolism of rat gastrointestinal tract. Gut 37(3):353–360PubMedPubMedCentralCrossRefGoogle Scholar
  118. 118.
    King T, Pusztai A, Clarke E (1980) Kidney bean (Phaseolus vulgaris) lectin-induced lesions in rat small intestine: 1. Light microscope studies. J Comp Pathol 90(4):585–595PubMedCrossRefPubMedCentralGoogle Scholar
  119. 119.
    Miyake K, Tanaka T, Mcneil PL (2007) Lectin-based food poisoning: a new mechanism of protein toxicity. PLoS One 2(8):e687PubMedPubMedCentralCrossRefGoogle Scholar
  120. 120.
    Pusztai A, Palmer R (1977) Nutritional evaluation of kidney beans (Phaseolus vulgaris): the toxic principle. J Sci Food Agric 28:620–623CrossRefGoogle Scholar
  121. 121.
    Vasconcelos IM, Oliveira JTA (2004) Antinutritional properties of plant lectins. Toxicon 44(4):385–403PubMedCrossRefPubMedCentralGoogle Scholar
  122. 122.
    Rougé P, Culerrier R, Granier C, Rancé F, Barre A (2010) Characterization of IgE-binding epitopes of peanut (Arachis hypogaea) PNA lectin allergen cross-reacting with other structurally related legume lectins. Mol Immunol 47(14):2359–2366PubMedCrossRefPubMedCentralGoogle Scholar
  123. 123.
    Brash AR (1999) Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate. J Biol Chem 274:23679–23682PubMedCrossRefPubMedCentralGoogle Scholar
  124. 124.
    Porta H, Rocha-Sosa M (2002) Plant lipoxygenases, physiological and molecular features. Plant Physiol 130:15–21PubMedPubMedCentralCrossRefGoogle Scholar
  125. 125.
    Zhu-Salzman K, Salzman RA, Ahn JE, Koiwa H (2004) Transcriptional regulation of sorghum defense determinants against a phloem-feeding aphid. Plant Physiol 134(1):420–431PubMedPubMedCentralCrossRefGoogle Scholar
  126. 126.
    Moran PJ, Thompson GA (2001) Molecular responses to aphid feeding in Arabidopsis in relation to plant defense pathways. Plant Physiol 125(2):1074–1085PubMedPubMedCentralCrossRefGoogle Scholar
  127. 127.
    Mai VC, Drzewiecka K, Jeleń H, Narożna D, Rucińska-Sobkowiak R, Kęsy J, Floryszak-Wieczorek J, Gabryś B, Morkunas I (2014) Differential induction of Pisum sativum defense signaling molecules in response to pea aphid infestation. Plant Sci 221-222:1–12PubMedCrossRefPubMedCentralGoogle Scholar
  128. 128.
    Lenis JM, Gillman JD, Lee JD, Shannon JG, Bilyeu KD (2010) Soybean seed lipoxygenase genes: molecular characterization and development of molecular marker assays. Theor Appl Genet 120(6):1139–1149PubMedCrossRefPubMedCentralGoogle Scholar
  129. 129.
    Khokhar S, Owusu-Apenten RK (2003) Antinutritional factors in food legumes and effects of processing. In: Squires VR (ed) The role of food, agriculture, forestry and fisheries in human nutrition – Vol IV. Encyclopedia of Life Support Systems (EOLSS), Oxford, pp 82–116Google Scholar
  130. 130.
    Johnson IT, Gee JM, Price K, Curl C, Fenwick GR (1986) Influence of saponins on gut permeability and active nutrient transport in vitro. J Nutr 116(11):2270–2277PubMedCrossRefPubMedCentralGoogle Scholar
  131. 131.
    Anderson RL, Wolf WJ (1995) Compositional changes in trypsin inhibitors, phytic acid, saponins and isoflavones related to soybean processing. J Nutr 125:581S–585SPubMedPubMedCentralGoogle Scholar
  132. 132.
    El-Adaway TA (2002) Nutritional composition and antinutritional factors of chickpeas (Cicer arietinum L.) undergoing different cooking methods and germination. Plant Foods Hum Nutr 57(1):83–97CrossRefGoogle Scholar
  133. 133.
    Vadivel V, Janardhanan (2005) Nutritional and antinutritional characteristics of seven south Indian wild legumes. Plant Food Hum Nutr 60:69–75CrossRefGoogle Scholar
  134. 134.
    Kansal R, Kumar M, Kuhar K, Gupta IRN, Subrahmanyam B, Koundal KR, Gupta VK (2008) Purification and characterization of trypsin inhibitor from Cicer arietinum L. and its efficacy against Helicoverpa armigera Braz. J Plant Physiol 20(4):313–322Google Scholar
  135. 135.
    Balail NG (2014) Effect of De cortication and roasting on trypsin inhibitors and tannin contents of cowpea (Vigna unguiculata L. Walp) seeds. Pak J Biol Sci 17:864–867PubMedCrossRefPubMedCentralGoogle Scholar
  136. 136.
    Lin G, Bode W, Huber R, Chi C, Engh RA (1993) The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin. Eur J Biochem 212(2):549–555PubMedCrossRefPubMedCentralGoogle Scholar
  137. 137.
    Liener I (1979) Significance for humans of biologically active factors in soybeans and other food legumes. J Am Oil Chem Soc 56(3):121–129PubMedCrossRefPubMedCentralGoogle Scholar
  138. 138.
    Liener IE (1995) Possible adverse effects of soybean anticarcinogens. J Nutr 125(3):744S–750SPubMedPubMedCentralGoogle Scholar
  139. 139.
    Friedman M, Brandon DL (2001) Nutritional and health benefits of soy proteins. J Agric Food Chem 49:1069–1086PubMedCrossRefPubMedCentralGoogle Scholar
  140. 140.
    Lajolo FM, Genovese MI (2002) Nutritional significance of lectins and enzyme inhibitors from legumes. J Agric Food Chem 50(22):6592–6598PubMedCrossRefPubMedCentralGoogle Scholar
  141. 141.
    Pusztai A, Grant G, Bardocz S, Baintner K, Gelencser E, Ewen SWB (1997) Both free and complexed trypsin inhibitors stimulate pancreatic secretion and change duodenal enzyme levels. Am J Phys 35:G340–G350Google Scholar
  142. 142.
    Maneepun S (2003) Traditional processing and utilization of legumes in processing and utilization of legumes report of the APO seminar on processing and utilization of legumes, Japan, 9–14 Oct 2000 ©APO 2003, ISBN: 92-833-7012-0, pp 53–62Google Scholar
  143. 143.
    Khokhar S, Chauhan BM (1986) Antinutritional factors in moth bean (Vigna aconitifolia): varietal differences and effects of methods of domestic processing and cooking. J Food Sci 51(3):591–594CrossRefGoogle Scholar
  144. 144.
    Prabhakaran MP, Perera CO, Valiyaveettil S (2006) Effect of different coagulants on the isoflavone levels and physical properties of prepared firm tofu. Food Chem 99(3):492–499CrossRefGoogle Scholar
  145. 145.
    Noguchi A (2003) Modern processing and utilization of legumes – recent research and industrial achievements in soybean foods in Japan in processing and utilization of legumes report of the APO seminar on processing and utilization of legumes, Japan, 9–14 Oct 2000 ©APO 2003, ISBN: 92-833-7012-0, pp 63–74Google Scholar
  146. 146.
    Une S, Nonaka K, Akiyama J (2016) Effects of hull scratching, soaking, and boiling on Antinutrients in Japanese red sword bean (Canavalia gladiata). J Food Sci 81(10):C2398–C2404PubMedCrossRefPubMedCentralGoogle Scholar
  147. 147.
    Bau HM, Villaume C, Méjean L (2000) Effects of soybean (Glycine max) germination on biologically active components, nutritional values of seeds, and biological characteristics in rats. Nahrung 44(1):2–6PubMedCrossRefPubMedCentralGoogle Scholar
  148. 148.
    Khalil AH, Mansour EH (1995) The effect of cooking, autoclaving and germination on the nutritional quality of faba beans. Food Chem 54:177–182CrossRefGoogle Scholar
  149. 149.
    Fernandez-Lopez A, Lamothe V, Delample M, Denayrolles M, Bennetau-Pelissero C (2016) Removing isoflavones from modern soyfood: why and how? Food Chem 210:286–294PubMedCrossRefPubMedCentralGoogle Scholar
  150. 150.
    Liu Z, Li W, Sun J, Zeng Q, Huang J, Yu B, Huo J (2004) Intake of soy foods and soy isoflavones by rural adult women in China. Asia Pac J Clin Nutr 13(2):204–209PubMedPubMedCentralGoogle Scholar
  151. 151.
    Cassidy A, Bingham S, Setchell KD (1994) Biological effects of a diet of soy protein rich in isoflavones on the menstrual cycle of premenopausal women. Am J Clin Nutr 60(3):333–340PubMedCrossRefPubMedCentralGoogle Scholar
  152. 152.
    Chen KI, Erh MH, Su NW, Liu WH, Chou CC, Cheng KC (2012) Soyfoods and soybean products: from traditional use to modern applications. Appl Microbiol Biotechnol 96(1):9–22PubMedCrossRefPubMedCentralGoogle Scholar
  153. 153.
    Hotz C, Gibson RS (2007) Traditional food-processing and preparation practices to enhance the bioavailability of micronutrients in plant-based diets. J Nutr 137(4):1097–1100PubMedCrossRefPubMedCentralGoogle Scholar
  154. 154.
    Lönnerdal B, Sandberg A-S, Sandström B, Kunz C (1989) Inhibitory effects of phytic acid and other inositol phosphates on zinc and calcium absorption in suckling rats. J Nutr 119:211–214PubMedCrossRefPubMedCentralGoogle Scholar
  155. 155.
    Sandberg A-S, Brune M, Carlsson N-G, Hallberg L, Skoglund E, Rossander-Hulthen L (1999) Inositol phosphates with different numbers of phosphate groups influence iron absorption in humans. Am J Clin Nutr 70:240–246PubMedCrossRefPubMedCentralGoogle Scholar
  156. 156.
    Hurrell RF (2004) Phytic acid degradation as a means of improving iron absorption. Int J Vitam Nutr Res 74:445–452PubMedCrossRefPubMedCentralGoogle Scholar
  157. 157.
    Teucher B, Olivares M, Cori H (2004) Enhancers of iron absorption: ascorbic acid and other organic acids. Int J Vitam Nutr Res 74:403–419PubMedCrossRefPubMedCentralGoogle Scholar
  158. 158.
    Ibrahim SS, Habiba RA, Shatta AA, Embaby HE (2002) Effect of soaking, germination, cooking and fermentation on antinutritional factors in cowpeas. Nahrung 46(2):92–95PubMedCrossRefPubMedCentralGoogle Scholar
  159. 159.
    Siulapwa N, Mwambungu A (2014) Nutritional value of differently processed soybean seeds. Int J Res Agric Food Sci 2(6):8–16Google Scholar
  160. 160.
    Martín-Cabrejas MA, Sanfiz B, Vidal A, Mollá E, Esteban R, López-Andréu FJ (2004) Effect of fermentation and autoclaving on dietary fiber fractions and antinutritional factors of beans (Phaseolus vulgaris L.). J Agric Food Chem 52(2):261–266PubMedCrossRefPubMedCentralGoogle Scholar
  161. 161.
    Chen Y, Xu Z, Zhang C, Kong X, Hua Y (2014) Heat-induced inactivation mechanisms of Kunitz trypsin inhibitor and Bowman-Birk inhibitor in soymilk processing. Food Chem 154:108–116PubMedCrossRefPubMedCentralGoogle Scholar
  162. 162.
    Miyagi Y, Shinjo S, Nishida R, Miyagi C, Takamatsu K, Yamamoto T, Yamamoto S (1997) Trypsin inhibitor activity in commercial soybean products in Japan. J Nutr Sci Vitaminol (Tokyo) 43(5):575–580CrossRefGoogle Scholar
  163. 163.
    Landete MJ, Hernández T, Robredo S, Dueñas M, de Las RB, Estrella I, Muñoz R (2015) Effect of soaking and fermentation on content of phenolic compounds of soybean (Glycine max cv. Merit) and mung beans (Vigna radiata [L] Wilczek). Int J Food Sci Nutr 66(2):203–209CrossRefGoogle Scholar
  164. 164.
    Mahungu SM, Diaz-Mercado S, Li J, Schwenk M, Singletary K, Faller J (1999) Stability of isoflavones during extrusion processing of corn/soy mixture. J Agric Food Chem 47(1):279–284PubMedCrossRefPubMedCentralGoogle Scholar
  165. 165.
    Bennetau-Pelissero C (2017) Positive or negative effects of isoflavones: toward the end of a controversy. Food Chem 225:293–301PubMedCrossRefPubMedCentralGoogle Scholar
  166. 166.
    Bennetau-Pelissero (2013) Chapter 77: Isoflavonoids and phytoestrogenic activity. In: Ramawat KG, Merillon JM (eds) Natural products edition. Springer, Berlin/Heidelberg, pp 2381–2431CrossRefGoogle Scholar
  167. 167.
    Verma AK, Kumar S, Das M, Dwivedi PD (2013) A comprehensive review of legume allergy. Clin Rev Allergy Immunol 45(1):30–46PubMedCrossRefPubMedCentralGoogle Scholar
  168. 168.
    Maria John KM, Khan F, Luthria DL, Garrett W, Natarajan S (2017) Proteomic analysis of antinutritional factors (ANF’s) in soybean seeds as affected by environmental and genetic factors. Food Chem 218:321–329PubMedCrossRefPubMedCentralGoogle Scholar
  169. 169.
    Somoza ML, Blanca-Lopez N, Perez Alzate D, Garcimartin MI, Ruano FJ, Anton-Laiseca A, Canto G (2015) Allergy to legumes in adults: descriptive features. J Allergy Clin Immunol 135:AB254CrossRefGoogle Scholar
  170. 170.
    Eigenmann PA (2009) Mechanisms of food allergy. Pediatr Allergy Immunol 20:5–11PubMedCrossRefPubMedCentralGoogle Scholar
  171. 171.
    Astwood JD, Leach JN, Fuchs RL (1996) Stability of food allergens to digestion in vitro. Nat Biotechnol 14:1269–1273PubMedCrossRefPubMedCentralGoogle Scholar
  172. 172.
    Egger M, Mutschlechner S, Wopfner N, Gadermaier G, Briza P, Ferreira F (2006) Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 61(4):461–476PubMedCrossRefPubMedCentralGoogle Scholar
  173. 173.
    Rance F, Dutau G (1997) Practical strategy for the diagnosis of food allergies. Pediatr Pulmonol Suppl 16:228–229PubMedCrossRefPubMedCentralGoogle Scholar
  174. 174.
    Bouakkadia H, Boutebba A, Haddad I, Vinh J, Guilloux L, Sutra JP, Sénéchal H, Poncet P (2015) Immunoproteomics of non water-soluble allergens from 4 legumes flours: peanut, soybean, sesame and lentil. Ann Biol Clin 73(6):690–704Google Scholar
  175. 175.
    Verma AK, Kumar S, Das M, Dwivedi PD (2012) Impact of thermal processing on legume allergens. Plant Foods Hum Nutr 67(4):430–441PubMedCrossRefPubMedCentralGoogle Scholar
  176. 176.
    Davis PJ, Williams SC (1998) Protein modification by thermal processing. Allergy 53:102–105PubMedCrossRefPubMedCentralGoogle Scholar
  177. 177.
    Chung SY, Butts CL, Maleki SJ, Champagne ET (2003) Linking peanut allergenicity to the processes of maturation, curing, and roasting. J Agric Food Chem 51:4273–4277PubMedCrossRefPubMedCentralGoogle Scholar

Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department Life Science and HealthUniversity of BordeauxBordeauxFrance
  2. 2.Bordeaux Sciences AgroGradignanFrance

Personalised recommendations