This paper is a brief review of thermally induced covalent modifications to
proteins in foods, focussing mainly on the advanced glycation end-products
(AGE) of the Maillard reaction. Most foods are subjected to thermal proces
sing, either in the home or during their production/manufacture. Thermal pr
ocessing provides many beneficial effects, but also brings about major chan
ges in allergenicity. Far from being a general way to decrease allergenic r
isk, thermal processing is as likely to increase allergenicity as to reduce
it, through the introduction of neoantigens. These changes are highly comp
lex and not easily predictable, but there are a number of major chemical pa
thways that lead to distinct patterns of modification. Perhaps the most imp
ortant of these is through the reaction of protein amino groups with sugars
, leading to an impressive cocktail of AGE-modified protein derivatives. Th
ese are antigenic and many of the important neoantigens found in cooked or
stored foods are probably such Maillard reaction products. A deeper underst
anding of thermally induced chemical changes is essential for more advanced
risk assessments, more effective QC protocols, production of more relevant
diagnostic allergen extracts and the development of novel protein engineer
ing and therapeutic approaches to minimise allergenic risk.