Impact of Thermal Processing on Legume Allergens
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Food induced allergic manifestations are reported from several parts of the world. Food proteins exert their allergenic potential by absorption through the gastrointestinal tract and can even induce life threatening anaphylaxis reactions. Among all food allergens, legume allergens play an important role in induction of allergy because legumes are a major source of protein for vegetarians. Most of the legumes are cooked either by boiling, roasting or frying before consumption, which can be considered a form of thermal treatment. Thermal processing may also include autoclaving, microwave heating, blanching, pasteurization, canning, or steaming. Thermal processing of legumes may reduce, eliminate or enhance the allergenic potential of a respective legume. In most of the cases, minimization of allergenic potential on thermal treatment has generally been reported. Thus, thermal processing can be considered an important tool by indirectly prevent allergenicity in susceptible individuals, thereby reducing treatment costs and reducing industry/office/school absence in case of working population/school going children. The present review attempts to explore various possibilities of reducing or eliminating allergenicity of leguminous food using different methods of thermal processing. Further, this review summarizes different methods of food processing, major legumes and their predominant allergenic proteins, thermal treatment and its relation with antigenicity, effect of thermal processing on legume allergens; also suggests a path that may be taken for future research to reduce the allergenicity using conventional/nonconventional methods.
KeywordsThermal processing Legume allergens Neoantigen. IgE-binding proteins
Instantaneous controlled pressure-drop (detente instantanee controlee)
Sodium dodecyl sulphate polyacrylamide gel electrophoresis
Thanks are due to SIP-08 of Council of Scientific and Industrial Research (CSIR), New Delhi for financial support. We are thankful to Sakshi Mishra for editorial assistance. Alok Kumar Verma and Sandeep Kumar are thankful to CSIR, New Delhi for the award of their Senior Research Fellowships. This is CSIR-IITR manuscript # 3029.
Conflicts of interest
The authors have declared no conflict of interest.
- 2.Kumar S, Verma AK, Das M, Dwivedi PD (2012) Allergenic diversity among plant and animal food proteins. Food Rev Int 28:277–298Google Scholar
- 4.Verma AK, Kumar S, Das M, Dwivedi PD (2012) A comprehensive review of legume allergy. Clin Rev Allergy Immunol. doi: 10.1007/s12016-012-8310-6
- 7.Kumar S, Verma AK, Misra A, Tripathi A, Chaudhari BP, Prasad R, Jain SK, Das M, Dwivedi PD (2011) Allergenic responses of red kidney bean (Phaseolus vulgaris cv chitra) polypeptides in BALB/c mice recognized by bronchial asthma and allergic rhinitis patients. Food Res Int 44:2868–2879CrossRefGoogle Scholar
- 9.Chung SY, Reed S (2011) Removing peanut allergens by tannic acid. Food Chem 134:1468–1473Google Scholar
- 22.Kilara A, Harwalkar VR (1996) Denaturation. In: Nakai S, Modler HW (eds) Food proteins: properties and characterisation. VCH, New York, pp 71–165Google Scholar
- 36.Dalal I, Binson I, Reifen R, Amitai Z, Shohat T, Rahmani S, Levine A, Ballin A, Somekh E (2002) Food allergy is a matter of geography after all: Sesame as a major cause of severe IgE-mediated food allergic reactions among infants and young children in Israel. Allergy 57:362–365CrossRefGoogle Scholar
- 43.Ibanez MD, Martinez M, Sanchez JJ, Fernandez-Caldas E (2003) Legume: Cross-reactivity. Allergol Immunopathol 31:151–161Google Scholar
- 61.Kumar S, Verma AK, Das M, Dwivedi PD (2012) Molecular mechanism of IgE mediated food allergy. Int Immunopharmacol. doi: 10.1016/j.intimp.2012.05.018
- 62.van Regenmortel MHV (1992) Molecular dissection of protein antigens. In: van Regenmortel MHV (ed), Structure of Antigens, vol 1. CRC Press Inc, Massachusetts, pp 1–28Google Scholar
- 71.Maleki SJ, Hurlburt BK (2004) Structural and functional alterations in major peanut allergens caused by thermal processing. J AOAC Int 87:1475–1479Google Scholar
- 79.International Union of Immunological Societies Allergen Nomenclature (2007) IUIS official list http://www.allergen.org/List.htm
- 83.Guillamón E, Burbano C, Cuadrado C, Muzquiz M, Pedrosa MM, Sánchez M, Cabanillas B, Crespo JF, Rodriguez J, Haddad J, Allaf K (2008) Effect of an instantaneous controlled presssure drop on in vitro allergenicity to lupins (Lupinus albus var Multolupa). Int Arch Allergy Immunol 145:9–14CrossRefGoogle Scholar
- 88.Wilson S, Blaschek K, de Mejia E (2005) Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 63:47–58Google Scholar
- 95.Pastorello EA, Pravettoni V, Farioli L, Primavesi L, Scibilia J, Piantanida M, Mascheri A, Conti A (2010) Green bean (Phaseolus vulgaris): A new source of IgE- binding lipid transfer protein. J Agric Food Chem 58:4513–4516Google Scholar
- 96.Pahud JJ, Schwarz K (1984) Research and development of infant formulae with reduced allergenic properties. Ann Allergy 53:609–614Google Scholar