Maillard reaction in food allergy: Pros and cons

Abstract

Food allergens have a notable potential to induce various health concerns in susceptible individuals. The majority of allergenic foods are usually subjected to thermal processing prior to their consumption. However, during thermal processing and long storage of foods, Maillard reaction (MR) often takes place. The MR is a non-enzymatic glycation reaction between the carbonyl group of reducing sugars and compounds having free amino groups. MR may sometimes be beneficial by damaging epitope of allergens and reducing allergenic potential, while exacerbation in allergic reactions may also occur due to changes in the motifs of epitopes or neoallergen generation. Apart from these modulations, non-enzymatic glycation can also modify the food protein(s) with various type of advance glycation end products (AGEs) such as Nϵ-(carboxymethyl-)lysine (CML), pentosidine, pyrraline, and methylglyoxal-H1 derived from MR. These Maillard products may act as immunogen by inducing the activation and proliferation of various immune cells. Literature is available to understand pathogenesis of glycation in the context of various diseases but there is hardly any review that can provide a thorough insight on the impact of glycation in food allergy. Therefore, present review explores the pathogenesis with special reference to food allergy caused by non-enzymatic glycation as well as AGEs.

Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

“…The immunomodulatory effects of AGEs structures have been described in literature (reviewed in refs. ). For instance, the effects of MR on immunogenicity and allergenicity of food allergen OVA have also been studied and have shown an elevated risk of food allergy .…”

Peanut Allergy: Characteristics and Approaches for Mitigation

“…The modifications by thermal processing include altered tertiary and secondary structures of the native proteins (Maleiki, ; Maleki et al, ; Nesbit et al, ; Zhang, Zhu, Zhang, Cai, & Chen, ), consequently altering the allergenic potency to varying degrees. One of the mechanisms for reduction in IgE reactivity/allergenicity by heat processing is due to the disruption of conformational epitopes that lowers IgE binding, while the increase in IgE reactivity may be due to the exposure or generation of new epitopes (neo‐allergen) (Gupta et al., ; Maleki, Chung et al., ).…”

“…Enzymatic hydrolysis and hurdle techniques have the greatest potential to alter allergenic proteins while covalent modifications such as crosslinking, aggregation, oxidation, reduction, alkylation, and acylation also impart significant alteration in allergenicity (Cabanillas et al., ; Chung & Champagne, ; Kasera, Singh, Lavasa, Prasad, & Arora, ; Mikiashvili & Yu, ; Yu, Ahmedna, Goktepe, Cheng, & Maleki, ). Some processing treatment methods may lead to an increase in IgE reactivity and produce unknown complexes (neoallergen) in peanut as an effect of the Maillard reaction (Gupta et al., ; Kumar, Verma, Das, & Dwivedi, ; Maleki, Chung, Champagne, & Raufman, ). Destruction of conformational epitopes may expose masked epitopes while linear epitopes may be altered by chemical and enzymatic hydrolysis (Kasera et al., ; Lee et al., ; Rahaman et al., ).…”

Germ-free mice exhibit mast cells with impaired functionality and gut homing and do not develop food allergy

“…In our study, GF animals were fed by γ -irradiated chow, which is in contrast to sterilization method used by Cahenzli et al, where the chow was autoclaved (Cahenzli, Köller et al 2013). Autoclaving leads to formation of advanced glycation end- products as a result of chemical reaction between reducing sugars and amino acids in proteins or lipides (Meillard reaction) (Gupta, Gupta et al 2016). These products has been recently pointed at as one of the possible causes of increasing FA incidence in Western countries (Smith 2017).…”