Characterization of Protein Fractions

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Proteomics has been used to identify proteins in a variety of subfractions of wheat endosperm or flour. Salt et al. [47] identified foam-forming proteins from wheat flour doughs that may play roles in stabilizing gas bubbles in dough and influencing the crumb structure of bread. Of the 42 proteins identified, the most abundant were a-amylase/trypsin inhibitors, tritin, serpins, and ^-amylase. Amiour et al. [12, 48] identified nearly 100 proteins in a fraction containing amphiphilic proteins linked to dough quality. Using multiple-regression analysis, puroindoline a and b, dehy-drin, POX, CHS, and RIP were determined to be significantly associated with grain hardness, an important quality attribute. Wong et al. [37] identified proteins in a salt-soluble, methanol-soluble endosperm fraction. The principal proteins in this fraction were a-amylase inhibitors and a-amylase/trypsin inhibitors, proteins historically designated as CM proteins [49], as well as some gliadins. Most of the proteins in this fraction contain conserved cysteines and are potential targets of thioredoxin [36]. Reduction of these proteins by thioredoxin altered their solubility, supporting the view that mobilization of seed reserves is promoted by a thioredoxin-linked signaling mechanism [38].

Allergen Identification

Proteomics offers an effective approach for identifying wheat allergens. 2-DGE was coupled with Edman microsequencing [50, 51] or MS [52] to identify wheat proteins involved in baker's asthma, an IgE-mediated allergy. Proteins that cross-reacted with sera from asthmatic patients include a-amylase inhibitor [50, 51]; GAPDH, TPI, and serpin [52]; and acyl-CoA oxidase and FBA [51]. Wheat food allergies are also IgE-mediated; proteins that cross-react with sera from allergic patients include lipid transfer protein (LTP) as well as a-, P-, y-, and «-gliadins [53]. Proteomic procedures are also being developed for the screening of allergens with S-S bonds [54]. Allergen research appears to be an especially promising area for applying proteomics to identify and characterize allergens in foods and food products.

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