Bos d 11 in baked milk poses a risk for adverse reactions in milk‐allergic patients

Abstract

Cow's milk allergy is the most common form of food allergy, affecting around 1%-4% of young children in Europe and other Western countries. 1-3 Milk allergy is caused by an adverse immune reaction to one or more of the proteins in cow's milk. Approximately 50% of these reactions are IgE-mediated and, in the most severe cases, are associated with anaphylaxis. Although it is arguable whether the prevalence of childhood milk allergy has increased in recent years, there is some evidence that allergic reactions to cow's milk have become more persistent. 4,5 Most milk-allergic children (80%) outgrow the condition by the time of school age and develop clinical tolerance to cow's milk allergens. However, some children have more severe phenotypes associated with high IgE levels and IgE antibodies to casein and may not develop tolerance until adolescence or, in the most severe cases, into adulthood. 6 The patterns of sensitization to individual cow's milk proteins varies significantly by study population and age. 6,7 Approximately 61% of cow's milk reactive individuals

Milk ladder as a therapeutic option for cow’s milk allergy: Proposal for a step-by-step plan for cow’s milk introduction in cow’s milk allergy

“…An important prerequisite for its use is that parents have a good understanding of the implementation and principle of the milk ladder and can put it into practice. Otherwise, it carries the risk of allergic reactions, for example, by advancing too quickly on the ladder or by the premature consumption of products that are not well baked [ 13 , 23 ]. In addition, in the authors’ experience, the risk of an allergic reaction is particularly increased during the transition from long-baked to rather short-heated products, e.g., from muffin to pancake.…”

“…Exposure to heat leads to denaturation of the conformational epitopes, while linear epitopes tend to remain intact. The individual protein fractions in cow’s milk react differently to heat: casein is widely heat stable, whereas α-lactalbumin and β-lactoglobulin are heat labile [ 23 ]. Conformational epitopes of β-lactoglobulin can be reduced by 99% from 680 µg in a muffin batter to 0.17 µg in a baked muffin [ 26 ].…”

Food allergen ladders: A need for standardization

“…Ladders are developed based on the theoretical knowledge that increased and prolonged heating in the presence of a wheat (grain) matrix reduces the allergenicity of the food protein by inhibiting binding to conformational epitopes. 24…”

“…Other aspects of processing, such as enzymes used in cheese making and bacteria used in yogurt production, may also affect allergenicity but have not been well studied. Ladders are developed based on the theoretical knowledge that increased and prolonged heating in the presence of a wheat (grain) matrix reduces the allergenicity of the food protein by inhibiting binding to conformational epitopes 24 …”

“…Hindley et al 24 recently demonstrated that Bos d 5 (beta‐lactoglobulin; conformational epitopes) levels were reduced from 680 µg/g in an unbaked muffin mix to 0.17 µg/g in baked muffins, indicating >99% decrease after baking. However, the casein/linear proteins in milk (Bos d 11) remained high even in the baked muffin and only decreased by 30% from a mean of 4249 µg/g in the unbaked muffin mix to 2961 µg/g when baked (~181 mg Bos d 11 per muffin).…”