Effect of an instantaneous controlled pressure drop on in vitro allergenicity to lupins (Lupinus albus var Multolupa)

International Archives of Allergy and Immunology

Volumn 145, Issue 1, 2008, Pages 9-14

  Guillamón, Eva ^a   Burbano, Carmen ^a   Cuadrado, Carmen ^a   Muzquiz, Mercedes ^a   Pedrosa, Mercedes M ^a   Sánchez, Mónica ^b   Cabanillas, Beatriz ^b   Crespo, Jesus F ^b   Rodriguez, Julia ^b   Haddad, Joshep ^c   Allaf, Karin ^c  

^a INIA   (Spain)

^b HOSPITAL UNIVERSITARIO 12 DE OCTUBRE   (Spain)

^c UNIVERSITÉ DE LA ROCHELLE   (France)

Author keywords

DIC ; Food allergy; In vitro IgE binding; Instantaneous controlled pressure drop; Lupinus albus; Thermal processing

Indexed keywords

ALLERGENICITY; ARTICLE; COTYLEDON; IMMUNOREACTIVITY; LUPIN; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRESSURE; PRIORITY JOURNAL; PROTEIN MODIFICATION; SENSITIZATION; SOLUBILITY; WESTERN BLOTTING;

EID: 37249009543     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000107461     Document Type: Article

References (42)

1. Duranti M: Grain legume proteins and nutraceutical properties. Fitoterapia 2006;77:67-82.
2. Yanez E, Ivanovic D, Owen DF, Ballester D: Chemical and nutritional evaluation of sweet lupines. Ann Nutr Metab 1983;27:513-520.
3. Lee YP, Mori TA, Sipsas S, Barden A, Puddey IB, Burke V, Hall RS, Hodgson JM: Lupin-enriched bread increases satiety and reduces energy intake acutely. Am J Clin Nutr 2006;84:975-980.
4. Wittig PE, Carreno P, Urrutia X, López L, Ballester D: Sensory evaluation and acceptability of cookies enriched with sweet lupine (Lupinus albus cv Multolupa). J Food Sci 1987;52:1434-1435.
5. Drakos A, Doxastakis G, Kiosseoglou V: Functional effects of lupin proteins in comminuted meat and emulsion gels. Food Chem 2007;100:650-655
6. Duranti M, Restani P, Poniatowska M, Cerletti P: The seed globulins of Lupinus albus. Phytochemistry 1981;20:2071-2075.
7. Sirtori CR, Lovati MR, Manzoni C, Castiglioni S, Duranti M, Magni C, Morandi S, D'Agostina A, Arnoldi A: Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells. J Nutr 2004;134:18-23.
8. Magni C, Sessa F, Accardo E, Vanoni M, Morazzoni P, Scarafoni A, Duranti M: Conglutin γ, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats. J Nutr Biochem 2004;15:646-650.
9. Hefle SL, Lemanske RF, Bush RK: Adverse reaction to lupine-fortified pasta. J Allergy Clin Immunol 1994;94:167-172.
10. Romano C, Ferrara A, Tarallo S: Allergic reaction to lupine seed (Lupinus albus). Allergy 1997;2:113-114.
11. Matheu V, de Barrio M, Sierra Z, Azzari C, Rossi ME, Vierucci A: Lupine-induced anaphylaxis. Ann Allergy Asthma Immunol 1999;83:406-408.
12. Fæste CK, Løvik M, Wiker HG, Egaas E: A case of peanut cross-allergy to lupine flour in a hot dog bread. Int Arch Allergy Immunol 2004;135:36-39.
13. Moneret-Vautrin DE, Guerin L, Kanny G, Flabbee J, Fremont S, Morisset M: Cross-allergenicity of peanut and lupine: the risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 1999;104:883-888.
14. Magni C, Herndl A, Sironi E, Scarafoni A, Ballabio C, Restani P, Bernardini R, Novembre E, Vierucci A, Duranti M: One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of Lupinus albus and other legume seeds. J Agric Food Chem 2005;53:4567-4571.
15. Crespo JF, Rodríguez J, Vives R, James JM, Reano M, Daroca P, Burbano C, Muzquiz M: Occupational IgE-mediated allergy after exposure to lupine seed flour. J Allergy Clin Immunol 2001;56:918-919.
16. Moneret-Vautrin DA, Kanny G, Morisser M, RancéF, Fardeau MF, Beaudouin E: Severe food anaphylaxis: 107 cases registered in 2002 by the Allergy Vigilance Network. Allergy Immunol (Paris) 2004;36:46-51.
17. Holden L, Fæste CK, Egaas E: Quantitative sandwich ELISA for the determination of lupine (Lupinus spp.) in foods. J Agric Food Chem 2005;53:5866-5871.
18. Ibáñez D, Martínez M, Marañon F, Fernández-Caldas E, Alonso E, Laso T: Specific IgE determinations to crude and boiled lentil (Lens culinaris) extracts in lentil-sensitive children and controls. Allergy 1999;54:1209-1214.
19. Sanchez-Monge R, Lopez-Torrejon G, Pascual CY, Varela J, Martin-Esteban M, Salcedo G: Vicilin and convicilin are potential major allergens from pea. Clin Exp Allergy 2004;34:1747-1753.
20. Shibasaki M, Suzuki S, Tajma S, Remoto H, Kuruome T: Allergenicity of major component proteins of soybean. Int Arch Allergy Appl Immunol 1980;61:441-448.
21. Maleki SJ, Chung SY, Champagne ET, Khalifah RC: The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol 2000;106:763-768.
22. 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.
23. Mondoulet L, Paty E, Drumare MF, Ah-Leung S, Scheinmann P, Willemot RM, Wal JM, Bernard H: Influence of thermal processing on the allergenicity of peanut proteins. J Agric Food Chem 2005;53:4547-4553.
24. Maleki SJ, Hurlburt BK: Structural and functional alterations in major peanut allergens caused by thermal processing (review). J AOAC Int 2004;87:1475-1479.
25. Venkatachalam M, Teuber SS, Roux KH, Sathe SK: Effects of roasting, blanching, autoclaving, and microwave heating on antigenicity of almond (Prunus dulcis L.) proteins. J Agric Food Chem 2002;50:3544-3548.
26. Brenna O, Pompei C, Ortolani C, Pravettoni V, Farioli L, Pastorello EA: Technological processes to decrease the allergenicity of peach juice and nectar. J Agric Food Chem 2000;48:493-497.
27. Malley A, Baecher L, Mackler B, Perlman F: The isolation of allergens from the green pea. J Allergy Clin Immunol 1975;56:282-290.
28. Duranti M, Sessa F, Scarafoni A, Bellini T, Dallocchio F: Thermal stabilities of lupin seed conglutin γ protomers and tetramers. J Agric Food Chem 2000;48:1118-1123.
29. 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.
30. 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.
31. Haddad J, Greiner R, Allaf K: Changes in phytate content of Lupinus albus and L. mutabilis seed during controlled instantaneous pressure drop treatment; in Muzquiz M, Hill GD, Cuadrado C, Pedrosa MM, Burbano C (eds): Recent Advances of Research in Antinutritional Factors in Legume Seeds and Oilseeds. Wageningen, Wageningen Academic Publisher, 2004, pp 333-336.
32. Haddad J, Allaf K: The inactivation of soybean trypsin inhibitors by hydro-thermomechanical treatment;in Muzquiz M, Hill GD, Cuadrado C, Pedrosa MM, Burbano C (eds): Recent Advances of Research in Antinutritional Factors in Legume Seeds and Oilseeds. Wageningen, Wageningen Academic Publisher, 2004, pp 329-332.
33. Haddad J, Muzquiz M, Allaf K: Treatment of lupin seed using the instantaneous controlled pressure drop technology to reduce alkaloid content. Food Sci Tech Int 2006;12:365-370.
34. AOAC: Official Methods of Analysis, ed 16. Washington, AOAC, 1995.
35. Mosse J: Nitrogen to protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content. J Agric Food Chem 1990;38:18-24.
36. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
37. Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979;76:4350-4354.
38. Lovrien R, Matulis D: Assays for total protein. Current Protocols in Protein Science. 2001, DOI:10.1002/0471140864.ps0304s01.
39. Poms RE, Anklam E: Effects of chemical, physical, and technological processes on the nature of food allergens. J AOAC Int 2004;87:1466-1474.
40. Mills ENC, Huang L, Noel TR, Gunning AP, Morris VJ: Formation of thermally induced aggregates of the soya globulin beta-conglycinin. Biochim Biophys Acta 2001;1547:339-350.
41. Melo ST, Ferreira RB, Teixeira AN: The seed storage proteins from Lupinus albus. Phytochemistry 1994;37:641-648.
42. Magni C, Ballabio C, Restani P, Sironi E, Scarafoni A, Poiesi C, Duranti M: Two-dimensional electrophoresis and Western-blotting analyses with anti Ara h 3 basic subunit IgG evidence the cross-reacting polypeptides of Arachis hypogaea, Glycine max and Lupinus albus seed proteomes. J Agric Food Chem 2005;53:2275-2281.