Skip to main content
SpringerLink
Log in

Effect of DIC on the Allergenicity of Legume Proteins

  • Chapter
  • First Online:
Book cover Instant Controlled Pressure Drop (D.I.C.) in Food Processing

Part of the book series: Food Engineering Series ((FSES))

  • 1068 Accesses

Abstract

In recent years, legume proteins have gained importance as food ingredients because of their nutraceutical properties. However, legumes are also considered to be a prime factor in the development of food allergies. Peanuts and soybeans are major food allergens in Western countries; while lentil, chickpea, and lupine allergens are more relevant in the Mediterranean area. Moreover, lupine seed flour is increasingly used in bakery, snack, and pastry products due its multifunctional properties. Information about the effects of thermal processing indicates that treatments combining heat and steam pressure, like autoclaving and instant controlled pressure drop (DIC), could decrease allergenicity. This work reviews the effect of DIC treatment at several pressure and time conditions on lupine, peanut, lentil, chickpea, and soybean by SDS-PAGE and immunoblotting. The data demonstrate that DIC treatment decreases the overall in vitro IgE-binding capacity of peanut, lentil, and chickpea and markedly reduces lupine and soybean immunoreactivity.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Akkerdaas J, Finkina E, Balandin S, Santos Magadan S, Knulst A, Fernández-Rivas M, Asero R, van Ree R, Ovchinnikova T (2012) Lentil (Lens culinaris) lipid transfer protein Len c 3: a novel legume allergen. Int Arch Allergy Immunol 157(1):51–57. doi:10.1159/000324946

    Article  CAS  Google Scholar 

  • Álvarez-Álvarez J, Guillamón E, Crespo JF, Cuadrado C, Burbano C, Rodríguez J, Fernández C, Muzquiz M (2005) Effects of extrusion, boiling, autoclaving, and microwave heating on lupine allergenicity. J Agric Food Chem 53(4):1294–1298. doi:10.1021/jf0490145

    Article  Google Scholar 

  • Barre A, Jacquet G, Sordet C, Culerrier R, Rouge P (2007) Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts. Mol Immunol 44(12):3243–3255. doi:10.1016/j.molimm.2007.01.023

    Article  CAS  Google Scholar 

  • Besler M, Steinhart H, Paschke A (2001) Stability of food allergens and allergenicity of processed foods. J Chromatogr B Biomed Sci Appl 756:207–228

    Article  CAS  Google Scholar 

  • Beyer KB, Morrow E, X-M L, Bardina L (2001) Effects of cooking methods on peanut allergenicity. J Allergy Clin Immunol 107:1077–1081

    Article  CAS  Google Scholar 

  • Burks A, Williams L, Helm RM, Thresher W, Brooks J, Sampson H (1991) Identification of soy protein allergens in patients with atopic dermatitis and positive soy challenges: determination of change in allergenicity after heating or enzyme digestion. Adv Exp Med Biol 289:295–307

    Article  CAS  Google Scholar 

  • Burks A, Sampson H, Bannon G (1998) Peanut allergens. Allergy 53:725–730

    Article  CAS  Google Scholar 

  • Cabanillas B, Maleki SJ, Rodríguez J, Burbano C, Muzquiz M, Jimenez M, Pedrosa MM, Cuadrado C, Crespo JF (2012) Heat and pressure treatments effects on peanut allergenicity. Food Chem 132(1):360–366. doi:10.1016/j.foodchem.2011.10.093

    Article  CAS  Google Scholar 

  • Chung S-Y, Reed S (2011) Removing peanut allergens by tannic acid. Food Chem 134:1468–1473

    Article  Google Scholar 

  • Chung S, Butts C, Maleki SJ, Champagne E (2003) Linking peanut allergenicity to the processes of maturation, curing, and roasting. J Agric Food Chem 51:4273–4277

    Article  CAS  Google Scholar 

  • Commision Directive 2006/142/EC of the European Parlament and of the Council (2006) Official Journal of the European Union L 368/110.

    Google Scholar 

  • Crespo JF, Rodriguez J (2003) Food allergy in adulthood. Allergy 58:98–113

    Article  CAS  Google Scholar 

  • Crespo JF, Pascual C, Burks A, Helm R, Martín-Esteban M (1995) Frequency of food allergens in a paediatric population from Spain. Pediatr Allergy Immunol 6:39–43

    Article  CAS  Google Scholar 

  • Cuadrado C, Cabanillas B, Pedrosa MM, Varela A, Guillamón E, Muzquiz M, Crespo JF, Rodríguez J (2007) Effect of heat treatments on legume allergenicity. . Paper presented at the Integrating Legume Biology for Sustainable Agriculture. Proceedings of the 6th European Conference on Grain Legumes, Lisbon, Portugal, 12–16 November

    Google Scholar 

  • Cuadrado C, Cabanillas B, Pedrosa MM, Varela A, Guillamón E, Muzquiz M, Crespo JF, Rodríguez J, Burbano C (2009) Influence of thermal processing on IgE reactivity to lentil and chickpea proteins. Mol Nutr Food Res 53(11):1462–1468. doi:10.1002/mnfr.200800485

    Article  CAS  Google Scholar 

  • Cuadrado C, Cabanillas B, Pedrosa MM, Muzquiz M, Haddad J, Allaf K, Rodríguez J, Crespo JF, Burbano C (2011) Effect of instant controlled pressure drop on IgE antibody reactivity to peanut, lentil, chickpea and soybean proteins. Int Arch Allergy Immunol 156(4):397–404. doi:10.1159/000324443

    Article  CAS  Google Scholar 

  • Davis P, Williams S (1998) Protein modification by thermal processing. Allergy 53:102–105

    Article  CAS  Google Scholar 

  • Duranti M (2006) Grain legume proteins and nutraceutical properties. Fitoterapia 77:67–82

    Article  CAS  Google Scholar 

  • Duranti M, Sessa F, Scarafoni A, Bellini T, Dallocchio F (2000) Thermal stabilities of lupine seed conglutin ç protomers and tetramers. J Agric Food Chem 48:1118–1123

    Article  CAS  Google Scholar 

  • Endres J (ed) (2001) Soy protein products-characteristics, nutritional aspects, and utilization. AOCS, Champaign

    Google Scholar 

  • Guillamón E, Burbano C, Cuadrado C, Muzquiz M, Pedrosa MM, Sánchez M, Cabanillas B, Crespo JF, Rodríguez J, Haddad J, Allaf K (2008) Effect of an instantaneous controlled pressure drop on in vitro allergenicity to lupines (Lupinus albus var Multolupa). Int Arch Allergy Immunol 145(1):9–14. doi:10.1159/000107461

    Article  Google Scholar 

  • Guillamón E, Rodríguez J, Burbano C, Muzquiz M, Pedrosa MM, Cabanillas B, Crespo JF, Sancho A, Mills C, Cuadrado C (2010) Characterization of lupine major allergens (Lupinus albus L). Mol Nutr Food Res 54:1168–1676

    Article  Google Scholar 

  • Haddad J, Louka N, Gadouleau M, Juhel F, Allaf K (2001) Application du nouveau procédé de séchage/texturation par Détente Instantanée Contrôlée DIC aux poissons: impact sur les caractéristiques physico-chemiques du produit fini. Sci Aliment 21:481–498

    Article  CAS  Google Scholar 

  • Leterme P (2002) Recommendations by health organizations for pulse consumption. Br J Nutr 88:239–242

    Article  Google Scholar 

  • López-Torrejón G, Salcedo G, Martín-Esteban M, Diaz-Perales A, Pascual CY, Sánchez-Monge R (2003) Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. J Allergy Clin Immunol 112(6):1208–1215. doi:10.1016/j.jaci.2003.08.035

    Article  Google Scholar 

  • Maleki SJ (2004) Food processing: effects on allergenicity. Curr Opin Allergy Clin Immunol 4(3):241–245. doi:10.1097/00130832-200406000-00018

    Article  CAS  Google Scholar 

  • Maleki SJ, Chung SY, Champagne ET, Raufman JP (2000) The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol 106(4):763–768. doi:10.1067/mai.2000.109620

    Article  CAS  Google Scholar 

  • Mills C, Jenkins J, Marigheto N, Belton P, Gunning A, Morris V (2002) Allergens of the cupin superfamily. Biochem Soc Trans 30(6):925–929

    Article  CAS  Google Scholar 

  • Mills C, Jenkins JA, Alcocer M, Shewry P (2004) Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract. Crit Rev Food Nutr 44:379–407. doi:10.1080/104086904990489224

    Article  CAS  Google Scholar 

  • Mills C, Mackie A, Burney P, Beyer K, Frewer L, Madsen C, Botjes E, Crevel R, van Ree R (2007) The prevalence, cost and basis of food allergy across Europe. Allergy 62(7):717–722

    Article  CAS  Google Scholar 

  • Mondoulet L, Paty E, Drumare M-F, Sea A-L (2005) Influence of thermal processing on the allergenicity of peanut proteins. J Agric Food Chem 53:4547–4553

    Article  CAS  Google Scholar 

  • Moneret-Vautrin D, Guérin L, Kanny G, Flabbee J, Frémont S, Morisset M (1999) Cross-allergenicity of peanut and lupine: the risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 04(4 Pt 1):883–888

    Article  Google Scholar 

  • Mueller GA, Gosavi RA, Pomes A, Wuenschmann S, Moon AF, London RE, Pedersen LC (2011) Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity. Allergy 66(7):878–885. doi:10.1111/j.1398-9995.2010.02532.x

    Article  CAS  Google Scholar 

  • Niphadkar PV, Patil SP, Bapat MM (1997) Chickpea induced anaphylaxis. Allergy 52:480–482

    Article  Google Scholar 

  • Patil SP, Niphadkar PV, Bapat MM (2001) Chickpea: a major food allergen in the Indian subcontinent and its clinical and immunochemical correlation. Ann Allergy Asthma Immunol 87(2):140–145

    Article  CAS  Google Scholar 

  • Rabjohn P, Helm E, Stanley J, West C, Sampson H, Burks A, Bannon G (1999) Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 103:535–542

    Article  CAS  Google Scholar 

  • Sánchez-Monge R, Pascual CY, Díaz-Perales A, Fernández-Crespo J, Martín-Esteban M, Salcedo G (2000) Isolation and characterization of relevant allergens from boiled lentils. J Allergy Clin Immunol 106(5):955–961. doi:10.1067/mai.2000.109912

    Article  Google Scholar 

  • Sathe SK, Sharma GM (2009) Effects of food processing on food allergens. Mol Nutr Food Res 53(8):970–978. doi:10.1002/mnfr.200800194

    Article  CAS  Google Scholar 

  • Schmitt D, Nesbit J, Hurlburt B, Cheng H, Maleki SJ (2010) Processing can alter the properties of peanut extract preparations. J Agric Food Chem 58(2):1138–1143. doi:10.1021/jf902694j

    Article  CAS  Google Scholar 

  • Sicherer S, Sampson H (2007) Peanut allergy: emerging concepts and approaches for an apparent epidemic. J Allergy Clin Immunol 120(3):491–503

    Article  Google Scholar 

  • Thomas K, Herouet-Guicheney C, Ladics G, Bannon G, Cockburn A, Crevel R, Fitzpatrick J, Mills C, Privalle L, Vieths S (2007) Evaluating the effect of food processing on the potential human allergenicity of novel proteins: international workshop report. Food Chem Toxicol 45:1116–1122

    Article  CAS  Google Scholar 

  • Verma A, Kumar S, Das M, Dwivedi P (2012) A comprehensive review of legume. Clin Rev Allerg Immunol. doi:10.1007/s12016-012-8310-6

    Google Scholar 

  • Vioque J, Sánchez-Vioque R, Clemente A, Pedroche J, Bautista J, Millán F (1999) Purification and partial characterization of chickpea 2S albumin. J Agric Food Chem 47(4):1405–1409. doi:10.1021/jf980819k

    Article  CAS  Google Scholar 

  • Wal J (2003) Thermal processing and allergenicity of foods. Allergy 58:727–729

    Article  Google Scholar 

  • Wilson S, Blaschek K, Gonzalez de Mejia E (2005) Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 63:47–58

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Departamento de Tecnología de Alimentos, SGIT-INIA, Ctra. Coruña Km 7.5, 28040, Madrid, Spain

    Carmen Burbano & Carmen Cuadrado

Authors
  1. Carmen Burbano
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Carmen Cuadrado
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Carmen Burbano .

Editor information

Editors and Affiliations

  1. ABCAR-DIC Process, La Rochelle, France

    Tamara Allaf

  2. University of La Rochelle, La Rochelle, France

    Karim Allaf

Rights and permissions

Reprints and permissions

Copyright information

© 2014 Springer Science+Business Media New York

About this chapter

Cite this chapter

Burbano, C., Cuadrado, C. (2014). Effect of DIC on the Allergenicity of Legume Proteins. In: Allaf, T., Allaf, K. (eds) Instant Controlled Pressure Drop (D.I.C.) in Food Processing. Food Engineering Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-8669-5_4

Download citation

Publish with us

Policies and ethics

Search

Navigation