Open AccessIdentification and characterization of allergens in spices by mass spectrometry
Author(s) -
Hummel Marlene,
Wigger Tina,
Brockmeyer Jens
Publication year - 2014
Publication title -
clinical and translational allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.979
H-Index - 37
ISSN - 2045-7022
DOI - 10.1186/2045-7022-4-s2-p1
Subject(s) - medicine , identification (biology) , mass spectrometry , traditional medicine , chromatography , biology , chemistry , botany
Background One of the major sources of hidden allergens in food is the use of spices that contain undeclared allergenic ingredients. Sesame and mustard are highly relevant in this context, as both seeds are frequently used in a variety of spices and can elicit severe allergenic reactions. Major allergens of mustard and sesame belong to the 2S-albumin family of seed storage proteins. 2S-albumins are members of the prolamin superfamily and are widely distributed in seeds and tree nuts. 2S-albumins are synthesized as a single precursor protein with about 13 kDa size that is subjected to extensive posttranslational proteolytic processing. The mature 2S albumins are composed of two subunits of approximately 9-10 kDa and 3-4 kDa size, respectively, which are linked by disulfide bridges. The 2S albumins are encoded by a multigene family possibly leading to numerous isoforms that may show considerable differences in their structures and allergenicity. The precise number, amount and characteristics of 2S albumin isoforms present in mustard and sesame however still remain unclear. One characteristic modification found is the C-terminal clipping of the small subunit that has been exemplarily described for Ses i 1 [1].