Review
Stability of food allergens and allergenicity of processed foods

https://doi.org/10.1016/S0378-4347(01)00110-4Get rights and content

Abstract

The allergenicity of food could be altered by several processing procedures. For various foods of animal and plant origin the available literature on this alteration is described. Investigations on hidden allergens in food products are also dealt with.

Introduction

During the manufacture of food their allergenicity may be altered by various processing parameters. The allergenic activity may be unchanged, decreased or even increased by food processing. The molecular basis of changes in the allergenic activity is the inactivation or destruction of epitope structures or the formation of new epitopes or better access of cryptic epitopes by denaturation of the native allergen.

Table 1 gives an overview of important manufacturing procedures which potentially affect the allergenicity of food allergens. To date, there are only a few studies on alteration of the allergenicity of processed foods. Most studies were done with native foods or allergen extracts of native foods. Some studies were initially started by a single case of adverse reaction to a certain processed food without systematic investigations of processing parameters and without appropriate numbers of patients. There are a few model studies which imitate processing parameters listed in Table 1. Mainly heating (dry heating, boiling or cooking) and enzymatic digestions were investigated.

In the following, studies available in the literature will be described. It should be noted, that the “allergenicity” of food allergens was assessed in the minority of studies by double-blind placebo-controlled food challenge (DBPCFC). Most investigations were done by determination of the relative “IgE-binding potencies” of food allergens applying radio-allergosorbent test (RAST) or enzyme-allergosorbent test (EAST) and RAST or EAST inhibition tests, respectively.

In addition to alteration of allergenic potencies the problem of allergen contamination is present in processed foods. There are no reliable data on the frequency of contamination of processed foods with undeclared allergens. According to the report on control of foodstuffs by the Standing Committee for Foodstuffs of the European Union [1] 2.3% of 838 “milk-free” samples from six EU-member states contained undeclared milk proteins. Related frequencies for contaminated “egg-free” and “gluten-free” products were 1.3% in Germany (n=319) and 5.2% in ten EU-member states (n=1583), respectively. These data could not be generalised, because the majority of sampling was on the basis of suspicion and analytical methods varied from one participating laboratory to another.

Section snippets

Milk and milk products

The major allergens from cow’s milk are constituted by caseins (Bos d 8, 20–30 kDa) and whey proteins beta-lactoglobulin (Bos d 5, 18 kDa), alpha-lactalbumin (Bos d 4, 14 kDa) and serum albumine (Bos d 6, 67 kDa) [2].

Raw milk and processed milk

Host and Samuelsson [3] investigated the allergenic potential of raw milk, pasteurized milk (75°C, 15 s) and pasteurized and homogenized milk (60°C, 175 kg/cm2) in five cow’s milk allergic children. All samples were positive in skin prick test (SPT) and DBPCFC with a trend to

Peanut and peanut products

Major allergens from peanuts are Ara h 1 (vicilin, 63.5 kDa), Ara h 2 (conglutin, 17 kDa) and Ara h 3 (glycinin, 57 kDa). Ara h 4 is an isoallergen of Ara h3. Minor allergens are Ara h 5 (profilin,15 kDa) and two conglutinin-homologous proteins Ara h 6 (15 kDa) and Ara h 7 (15 kDa) [71].

Conclusions

The stability of allergens from animal origin and their impact as hidden allergens are summarized in Table 2. Milk and egg and products of these are characterized by high stability to heating and their common occurrence as hidden allergens in processed foods. Fish and crustaceae and products of these are heat stable while the significance as hidden allergens is low. The allergenic potential of meat and meat products is partially heat stable while the enzymic stability is relatively weak. Meat

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