Background: The use of legume seeds is being expanded in the food industry due to their excellent nutritional and technological properties. However, legumes have been considered causative agents of allergic reactions through ingestion. Previous studies indicated that processing methods combining heat and steam pressure, such as instant controlled pressure drop (DIC®), could decrease allergenicity. The aim of this study was to investigate the impact of DIC treatment on peanut, lentil, chickpea and soybean IgE antibody reactivity. Methods: Peanut, lentil, chickpea and soybeanseeds were subjected to DIC treatment at different pressure and time conditions (3 and 6 bar for 1 and 3 min). Control (raw) and DIC-treated extracts were analyzed by SDS-PAGE and immunoblotting using a serum pool from sensitized patients. Results: DIC treatment did not affect the total protein content of legume seeds. Nevertheless, modifications of protein profiles after DIC showed a general decrease in IgE binding to legume proteins that was correlated to a higher steam pressure and longer treatment. The immunoreactivity of soybean proteins was almost abolished with treatment at 6 bar for 3 min. Conclusions: The results demonstrated that DIC treatment produces a reduction in the overall in vitro IgE binding of peanut, lentil and chickpea and a drastic reduction in soybean immunoreactivity.

1.
Leterme P: Recommendations by health organizations for pulse consumption. Br J Nutr 2002;88:239–242.
2.
Scarafoni A, Magni C, Duranti M: Molecular nutraceutics as a mean to investigate the positive effects of legume seed proteins on human health. Trends Food Sci Technol 2007;18:454–463.
3.
Sicherer SH, Sampson HA: Peanut allergy: emerging concepts and approaches for an apparent epidemic. J Allergy Clin Immunol 2007;120:491–503.
4.
Burks AW, Sampson HA, Bannon GA: Peanut allergens. Allergy 1998;53:725–730.
5.
Burks AW, Williams LW, Helm RM, Connaughton C, Cockrell G, O’Brien T: Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 1991;88:172–179.
6.
Burks AW, Williams LW, Connaughton C, Cockrell G, O’Brien TJ, Helm RM: Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J Allergy Clin Immunol 1992;90:962–969.
7.
Rabjohn P, Helm EM, Stanley JS, West CM, Sampson HA, Burks AW, Bannon GA: Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 1999;103:535–542.
8.
Crespo JF, Pascual CY, Burks AW, Helm RM, Martin-Esteban M: Frequency of food allergy in a pediatric population from Spain. Pediatr Allergy Immunol 1995;6:9–43.
9.
Pascual CY, Fernandez-Crespo J, Sanchez-Pastor S, Padial MA, Diaz-Pena JM, Martin-Muñoz F, Martin-Esteban M: Allergy to lentils in Mediterranean pediatric patients. J Allergy Clin Immunol 1999;103:154–158.
10.
Martínez San Ireneo M, Ibañez Sandín MD, Fernández-Caldas E, Marañón Lizana F, Rosales Fletes MJ, Laso Borrego MT: Specific IgE levels to Cicer arietinum (chickpea) in tolerant and nontolerant children: evaluation of boiled and raw extracts. Int Arch Allergy Immunol 2000;121:137–143.
11.
Patil SP, Niphadkar PV, Bapat MM: Chickpea: a major food allergen in the Indian subcontinent and its clinical and immunochemical correlation. Ann Allergy Asthma Immunol 2001;87:140–145.
12.
Sánchez-Monge R, Pascual CY, Díaz-Perales A, Fernández-Crespo J, Martín-Esteban M, Salcedo G: Isolation and characterization of relevant allergens from boiled lentils. J Allergy Clin Immunol 2000;106:955–961.
13.
López-Torrejón G, Salcedo G, Martín-Esteban M, Díaz-Perales A, Pascual CY, Sánchez-Monge R: Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. J Allergy Clin Immunol 2003;112:1208–1215.
14.
Niphadkar PV, Patil SP, Bapat MM: Chickpea-induced anaphylaxis. Allergy 1997;52:115–116.
15.
Wilson S, Blaschek K, Gonzalez de Mejia E: Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 2005;63:47–58.
16.
Maruyama N, Fukada T, Saka S, Inui N, Kotoh J, Miyagawa M, Hayashi M, Sawada M, Moriyama T, Utsumi S: Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins. Phytochemistry 2003;64:701–708.
17.
Christensen HR, Bruun SW, Frokiaer H: Antigenic specificity of serum antibodies in mice fed soy protein. Int Arch Allergy Immunol 2003;132:58–67.
18.
Ogawa A, Samoto M, Takahashi K: Soybeans allergens and hypoallergenic soybean products. J Nutr Sci Vitaminol (Tokyo) 2000;46:271–279.
19.
Mills ENC, Sancho AI, Rigby NM, Jenkins JA, Mackie AR: Impact of food processing on the structural and allergenic properties of food allergens. Mol Nutr Food Res 2009;53:963–969.
20.
Paschke A: Aspects of food processing and its effect on allergen structure. Mol Nutr Food Res 2009;53:959–962.
21.
Sathe SK, Sharma GM: Effects of food processing on food allergens. Mol Nutr Food Res 2009;53:970–978.
22.
Besler M, Steinhart H, Paschke A: Stability of food allergens and allergenicity of processed foods. J Chromatogr B Biomed Sci Appl 2001;756:207–228.
23.
Álvarez-Álvarez J, Guillamón E, Crespo JF, Cuadrado C, Burbano C, Rodríguez J, Fernández C, Muzquiz M: Effects of extrusion, boiling, autoclaving and microwave heating on lupine allergenicity. J Agric Food Chem 2005;53:1294–1298.
24.
Cuadrado C, Cabanillas B, Pedrosa MM, Varela A, Guillamón E, Muzquiz M, Crespo JF, Rodríguez J, Burbano C: Influence of thermal processing on IgE reactivity to lentil and chickpea proteins. Mol Nutr Food Res 2009;53:1462–1468.
25.
Guillamón E, Burbano C, Cuadrado C, Muzquiz M, Pedrosa MM, Sánchez M, Cabanillas B, Crespo JF, Rodríguez J, Haddad J, Allaf K: Effect of an instantaneous controlled pressure drop on in vitro allergenicity to lupins (Lupinus albus var Multolupa). Int Arch Allergy Immunol 2008;145:9–14.
26.
Guillamón E, Rodríguez J, Burbano C, Muzquiz M, Pedrosa MM, Cabanillas B, Crespo JF, Sancho AI, Mills ENC, Cuadrado C: Characterization of lupin major allergens (Lupinus albus L). Mol Nutr Food Res 2010;54:1168–1676.
27.
Haddad J, Louka N, Gadouleau M, Juhel F, Allaf K: 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 2001;21:481–498.
28.
Haddad J, Greiner R, Allaf K: Effect of instantaneous controlled pressure drop on the phytate content of lupin. Swiss Soc Food Sci Technol 2007;40:448–453.
29.
AOAC: Official Methods of Analysis, ed 16. Washington, AOAC, 1995.
30.
Mossé J: Nitrogen to protein conversion factor for ten cereals and six legumes or oil-seed protein content. J Agric Food Chem 1990;38:18–24.
31.
Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680–685.
32.
Haddad J, Allaf K: Impact of controlled instantaneous pressure drop (DIC) on lupin quality; in Van Santen E, Wink M, Weissmann S, Römer P (eds): Wild and Cultivated Lupins from the Tropics to the Poles. Proceedings of the 10th International Lupin Conference. Canterbury, International Lupin Association, 2004, pp 368–371.
33.
Schmitt DA, Nesbit JB, Hurlburt BK, Cheng H, Maleki SJ: Processing can alter the properties of peanut extract preparations. J Agric Food Chem 2010;58:1138–1143.
34.
Beyer K, Morrow E, Li XM, Bardina L, Bannon GA, Burks AW, Sampson HA: Effects of cooking methods on peanut allergenicity. J Allergy Clin Immunol 2001;107:1077–1081.
35.
Koppelman SJ, Bruijnzeel-Koomen CA, Hessing M, de Jogh HH: Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol Chem 1999;274:4770–4777.
36.
Maleki SJ, Hurlburt BK: Structural and functional alterations in major peanut allergens caused by thermal processing (review). J AOAC Int 2004;87:1475–1479.
37.
Ibáñez Sandín D, Martínez San Ireneo M, Marañón Lizana F, Fernández-Caldas E, Alonso Lebrero E, Laso Borrego T: Specific IgE determinations to crude and boiled lentil (Lens culinaris) extracts in lentil-sensitive children and controls. Allergy 1999;54:1209–1214.
38.
Martínez San Ireneo M, Ibáñez MD, Fernández-Caldas E, Carnes J: In vitro and in vivo cross-reactivity studies of legume allergy in a Mediterranean population. Int Arch Allergy Immunol 2008;147:222–230.
39.
Burks AW, Williams LW, Helm RW, Thresher W, Brooks JR, Sampson HA: 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 1991;289:295–307.
40.
Cuadrado C, Cabanillas B, Pedrosa MM, Varela A, Guillamón E, Muzquiz M, Crespo JF, Rodriguez J: Effect of heat treatments on legume allergenicity. Integrating Legume Biology for Sustainable Agriculture: Proceedings of the 6th European Conference on Grain Legumes, Lisbon, 2007, pp 186–187.
41.
Thomas K, Herouet-Guicheney C, Ladics G, Bannon G, Cockburn A, Crevel R, Fitzpatrick J, Mills C, Privalle L, Vieths S: Evaluating the effect of food processing on the potential human allergenicity of novel proteins: international workshop report. Food Chem Toxicol 2007;45:1116–1122.
42.
Maleki SJ: Food processing: effects on allergenicity. Curr Opin Allergy Clin Immunol 2004;4:241–245.
Copyright / Drug Dosage / Disclaimer
Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.
You do not currently have access to this content.