BrahminBoss
Boatsman from river of Styx triple 6
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It had been well demonstrated earlier that cooking reduces the allergenicity of egg white proteins by altering the trypsin inhibitor which normally prevents complete digestion. The egg proteins when cooked properly appear to dissolve efficiently in vitro using enzymes you'd expect in the human stomach. I hope this study deals with lipids and not just heat. Here is a quote which confirms the allergenic increase upon heating seen in tropomyosin (a shell fish muscle protein):
'Heating generally decreases protein allergenicity by destroying conformational epitopes. In peanut and shrimp, heat-induced Maillard reaction (glycation) may increase allergenicity. The majority of milk and egg-allergic children tolerate extensively heated (baked with wheat matrix) milk and egg. Introduction of extensively heated milk and egg proteins is associated with decreasing sizes of skin prick test wheals and increasing serum food-specific IgG levels.'
Heating of β-lactoglobulin results in the formation of intermolecular disulfide bonds and subsequent binding to other food proteins, making β-lactoglobulin less allergenic. A recent study by Kato et al. [14] demonstrated a marked decrease in the solubility of ovomucoid when egg white was mixed with wheat flour and wheat gluten and then heated at 180°C for 10 min, mimicking the process of bread making. Immunoblotting suggested that ovomucoid polymerizes and forms high-molecular weight complexes with gluten leading to aggregation and insolublization of ovomucoid'
'Can heating enhance allergenicity? High temperature may enhance allergenicity of peanut and shrimp as a result of glycation, the Maillard reaction between free amino acids, and aldehyde or ketone groups of sugars. The Maillard reaction induces the formation of aggregates that are more resistant to gastric digestion and bind IgE antibody more effectively than unheated. For shellfish, such reactions may create new epitopes. However, in the case of other foods, glycation may result in decreased allergencity;'
Not only can cooking break bonds and reduce allergenicity, it can also creating new bonds and enhance it. If a person is allergic to omelets with American‐produced Emmentaler (A1 milk), this says little about what would happen after eating a boiled egg with pieces of goat‐derived or Swiss cheese (A2 milk). I still think that the matrix effects of an omelet would present more of an immunogenic risk than boiled eggs due to the lipids coating the epitopes, perhaps increasing their solubility in the lipid phase and trapping them within micelles—preserving them in more‐or‐less whole‐form until they reach the small intestine.. .
'Heating generally decreases protein allergenicity by destroying conformational epitopes. In peanut and shrimp, heat-induced Maillard reaction (glycation) may increase allergenicity. The majority of milk and egg-allergic children tolerate extensively heated (baked with wheat matrix) milk and egg. Introduction of extensively heated milk and egg proteins is associated with decreasing sizes of skin prick test wheals and increasing serum food-specific IgG levels.'
Heating of β-lactoglobulin results in the formation of intermolecular disulfide bonds and subsequent binding to other food proteins, making β-lactoglobulin less allergenic. A recent study by Kato et al. [14] demonstrated a marked decrease in the solubility of ovomucoid when egg white was mixed with wheat flour and wheat gluten and then heated at 180°C for 10 min, mimicking the process of bread making. Immunoblotting suggested that ovomucoid polymerizes and forms high-molecular weight complexes with gluten leading to aggregation and insolublization of ovomucoid'
'Can heating enhance allergenicity? High temperature may enhance allergenicity of peanut and shrimp as a result of glycation, the Maillard reaction between free amino acids, and aldehyde or ketone groups of sugars. The Maillard reaction induces the formation of aggregates that are more resistant to gastric digestion and bind IgE antibody more effectively than unheated. For shellfish, such reactions may create new epitopes. However, in the case of other foods, glycation may result in decreased allergencity;'
Not only can cooking break bonds and reduce allergenicity, it can also creating new bonds and enhance it. If a person is allergic to omelets with American‐produced Emmentaler (A1 milk), this says little about what would happen after eating a boiled egg with pieces of goat‐derived or Swiss cheese (A2 milk). I still think that the matrix effects of an omelet would present more of an immunogenic risk than boiled eggs due to the lipids coating the epitopes, perhaps increasing their solubility in the lipid phase and trapping them within micelles—preserving them in more‐or‐less whole‐form until they reach the small intestine.. .
