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Food allergens reactivity as affected by thermal processing

Identification

Key words food, allergen, thermal processing, inactivation
Latest version 2012/07/31
Completed by FRIP

How does it work?

Primary objective The heating process (pasteurization, sterilization) made with aim to inactivate microbes, can as side effect change the allergenic protein structure and influence the accessibility of special places in protein structure (epitopes) by antibody substance IgE that cause start up the allergenic reaction of the patient.
Working principle During thermal processes, such as pasteurization, sterilization, boiling and roasting, some reaction products are generated in foods. Between them, so called Maillard reaction products (protein amino groups vs. saccharides reaction) originate. Some of them can induce severe allergenic reaction [1]. In following text the effect of heating on allergenicity of different foods or individual allergens is briefly described. In most cases, the heating itself cannot de-allergize foods. In some exceptional cases, the lowering of allergenic reaction is described. But, in peanut roasting, this process substantially increased the allergenicity of the final product. Therefore, no general advice can be provided and each product should be considered as specific case.

Eggs. Egg white after boiling exhibited still detectable allergenic reaction as stated in [2]. Cooking of various food extracts including eggs with vinegar substantially decreased size of wheals in prick-to prick test in sensitized individuals [3].

Legumes. Boiled lentils extract kept its allergenicity [4]. Soybean globulin, when heated, lost partly its allergenicity [5].

Fish and seafood. Cooking of fish caused denaturation and conglomeration of proteins but some bands presented IgE binding in WB [6]. Canning of fish caused the reduction in IgE binding [7].

Meat and meat products. Allergenicity of pork sausages digested by using pepsin and trypsin considerably decreased after autoclave treatment, and were also maintained or decreased after enzyme treatment. Accordingly, autoclave treatment represents a promising processing technology for the reduction of the allergenicity of diverse food products [8].

Peanuts and other nuts. First studies on roasting of peanuts proved that this dry heat treatment generated Maillard reaction products that have much more IgE binding properties than untreated control [9], [10]. Roasting, autoclaving, blanching, microwave heating of almonds indicated antigenic stability of almond proteins when compared with that of the unprocessed nuts in ELISA and Western blot tests [11]. Hazelnut protein with molecular
weight less than 14 kDa presented high heat stability and was detected even after treatment at 185°C [12].

Fruits and vegetables. Heat sterilization of peach at 121 °C for 10 and 30 min, chemical lye peeling of fruits and ultra-filtration of juice through membranes with suitable cutoff were tested. The sterilization was not able to decrease the allergenicity of the Pru p 1 protein. Furthermore, the protein band was still present even after 60-min reaction with two different acidic proteases. The chemical lye peeling of fruits and ultra-filtration of juice through membranes with suitable cutoff decreased the major allergen of peach [13]. Chemical peeling, thermal treatment, and syruping processes were applied on different varieties of cherry. Chemical peeling successfully removed Pru av 3, a lipid transfer protein (LTP) responsible for allergy syndrome in patients without pollinosis. The syruping process removed almost all allergenic proteins [14].

Pasta, grain and bakery products. Model pasta samples (durum wheat) were dried at temperatures 20, 60, 85, 110 and 180 °C and cooked in boiling water. Digestion process together with previous heat treatment was not able to completely inactivate the IgE-reactive peptides [15]. Almost all proteins of rice were excluded or weakened in the process of boiling but IgE binding activity still remained even in hypoallergenic rice [16]. Wheat dough and the bread crumb and crust, before and after being in vitro digested were tested for presence of allergens [17]. During in vitro digestion, the IgE binding protein components of the unheated dough disappear. The bread crumb and crust isolated proteins saved IgE binding. The effects of baking must be taken into account in studying food allergies to wheat products.

Milk and milk proteins. Raw, pasteurized, and homogenized/pasteurized cow milk and hypoallergenic infant formula as a control were tested [18]. This work provided evidence that heat treatment increased ability of pasteurized and homogenized/pasteurized milk to evoke allergic reactions in patients allergic to milk.

Images
Additional effects Heating, besides the antimicrobial effect, has a positive effect on food digestibility, food structure and overall quality, namely for animal origin raw materials.
Important process parameters Holding time at temperature and temperature.
Important product parameters Composition of food matrix.

What can it be used for?

Products Eggs, Legumes, Fish and seafood, Meat and meat products, Peanuts and other nuts, Fruits and vegetables, Pasta, Grain and bakery products, Milk and milk proteins.
Operations Heat pasteurization, sterilization, boiling and roasting.
Solutions for short comings This datasheet can provide answer on simple question “How can heat treatment influence the allergenicity of different food products?”

What can it NOT be used for?

Products There is also negative experience with influence of heating on allergenicity of some foods. This is caused in most cases by the specific composition of food matrix that contains protein protective substances, e.g. dry heat roasting of peanut increases the allergenicity (tested on patients sensitized to peanut main allergenic protein).
Operations Not known.
Other limitations The food structure limits the heating intensity. We can destroy by heating present allergens but the food matrix is so “well done” that it cannot be eaten.
Risks or hazards The detailed extracted facts from literature (see above) provide evidence that the heating process in many cases cannot inactivate the allergenicity of present proteins. In several cases, the allergenicity is increased by heating.

Implementation

Maturity The deallergization of foods by heating is not applied yet due to its relation on given food matrix.
Modularity /Implementation There would be no problem with implementation of a heating process into the existing lines. The deallergization, can be considered as a side effect of heat pasteurization or sterilization.
Consumer aspects Not known.
Legal aspects Allergens presence labelling is under the EU legislation regulation. No special legislation on labelling of the heat treated product is presented.

The EFSA Journal (2004) 32, 1 – 197; Opinion of the Scientific Panel on Dietetic Products, Nutrition and Allergies on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes Directive 2003/89/EC of the European Parliament and of the Council of 10 November 2003 Directive 2000/13/EC of the European Parliament and of the Council of 20 March 2000 Directive 2006/142/EC of the European Parliament and of the Council of 22 December 2006 Directive 2005/26/EC of the European Parliament and of the Council of 21 March 2005

Environmental aspects Not known.

Further Information

Institutes FRIP, IFR, University of Vienna, Dermatologische Klinik Universitätsspital Zürich, Paul-Ehrlich-Institut_Allergology division, JRC Geel_Inst Ref Mat and Measurements, University of Hamburg, USDA - ARS - SRRC, INRA - UIAA
Companies
References [1] Davis P.J., Smales C.M., James D.C.(2001). How can thermal processing modify the antigenicity of proteins? Allergy, 56 Suppl 67, 56-60

[2] Hoffman, D.R., (1983). Immunochemical identification of the allergens in egg white, Journal of Allergy and Clinical Immunology 71, 481-486

[3] Armentia, A. , Dueñas-Laita, A. , Pineda, F. , Herrero, M. , Martín, B.Vinegar decreases allergenic response in lentil and egg food allergy, (2010) Allergologia et Immunopathologia, 38 (2), 74-77.

[4] Ibáñez Sandín, D., Martínez San Ireneo, M., Maranõón Lizana, F., Fernández-Caldas, E., Alonso Lebrero, E., Laso Borrego, T. (1999). Specific IgE determinations to crude and boiled lentil (Lens culinaris) extracts in lentil-sensitive children and controls, Allergy: European Journal of Allergy and Clinical Immunology, 54, 1209-1214.

[5] Shibasaki, M., Suzuki, S., Tajima, S., Nemoto, H., Kuroume, T., (1980). Allergenicity of major component proteins of soybean, International Archives of Allergy and Applied Immunology, 61 (4), 441-448.

[6] Bernhisel-Broadbent, J., Scanlon, S.M., Sampson, H.A. (1992). Fish hypersensitivity. I. In vitro and oral challenge results in fish- allergic patients, Journal of Allergy and Clinical Immunology, 89, 730-737

[7] Bernhisel-Broadbent, J., Strause, D., Sampson, H.A. (1992). Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods, Journal of Allergy and Clinical Immunology, 90, 622-629.

[8] Kim, S.-J., Kim, K.-B.-W.-R., Song, E.-J., Lee, S.-Y., Yoon, S.-Y., Lee, S.-J., Lee, C.-J., Ann, D.H. (2009). Effect of digestive enzymes on the allergenicity of autoclaved market pork sausages, Korean Journal for Food Science of Animal Resources, 29 (2), 238-244.

[9] Maleki, S.J., Chung, S.-Y., Champagne, E.T., Raufman, J.-P. (2000). The effects of roasting on the allergenic properties of peanut proteins, Journal of Allergy and Clinical Immunology, 106, 763-768.

[10] Chung, S.Y., Champagne, E.T. (1999). Allergenicity of Maillard reaction products from peanut proteins, Journal of Agricultural and Food Chemistry, 47, 5227-5231.

[11] Venkatachalam, M., Teuber, S.S., Roux, K.H., Sathe, S.K., (2002). Effects of roasting, blanching, autoclaving, and microwave heating on antigenicity of almond (Prunus dulcis L.) proteins, Journal of Agricultural and Food Chemistry, 50, 3544-3548.

[12] Wigotzki, M., Steinhart, H., Paschke, A., (2000). Influence of varieties, storage and heat treatment on IgE-binding proteins in hazelnuts (Corylus avellana), Food and Agricultural Immunology, 12, 217-229.

[13] Brenna, O., Pompei, C., Ortolani, C., Pravettoni, V., Farioli, L., Pastorello, E.A. (2000). Technological processes to decrease the allergenicity of peach juice and nectar, Journal of Agricultural and Food Chemistry, 48, 493-497.

[14] Primavesi, L. , Brenna, O.V., Pompei, C. , Pravettoni, V. , Farioli, L. , Pastorello, E.A. (2006). Influence of cultivar and processing on cherry (Prunus avium) allergenicity, Journal of Agricultural and Food Chemistry, 54 , 9930-9935.

[15] De Zorzi, M., Curioni, A., Simonato, B., Giannattasio, M., Pasini, G., (2007). Effect of pasta drying temperature on
gastrointestinal digestibility and allergenicity of durum wheat proteins, Food Chemistry, 104 (1), 353-363.

[16] Yum, H.-Y., Lee, K.E., Choi, S.Y., Yang, H.S., Sohn, M.H., Kim, K.-E., Lee, S.-I. (2006). Wild rice, hypoallergenic rice - Immunologic comparison, Allergy and Asthma Proceedings, 27 (4), 387-392

[17] Simonato, B., Pasini, G., Giannattasio, M., Peruffo, A.D.B., De Lazzari, F., Curioni, A. (2001). Food allergy to wheat products: The effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust, Journal of Agricultural and Food Chemistry, 49, 5668-5673.

[18] Host,A., Samuelsson,E.G.,(1988).Allergic reactions to raw, pasteurized, and homogenized/pasteurized cow milk: a comparison. Allergy, 43, 113–118.



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Created by IeselVdP on 22 September 2011, at 19:44