Submitted to: Internet Web Page
Publication Type: Research Notes
Publication Acceptance Date: 10/18/2011
Publication Date: 10/18/2011
Citation: Mattison, C.P., Tarver, M.R., Desormeaux, W.A. 2011. Low molecular weight anti-carboxymethyl lysine reactive bands in cashew extracts. Internet Web Page. AB CAM Website. Interpretive Summary:
Technical Abstract: The Maillard Reaction is the non-enzymatic browning of foods during thermal processing, and is a result of the reaction of reducing sugar carbonyl groups and primary amine groups of proteins. Maillard Reaction products are unstable, and Amadori rearrangements result in a network of chemical modifications that have been termed Advanced Glycation Endproducts (AGEs). The Maillard reaction is favored under conditions of low moisture, high temperature, and high pH, and is important in creating the favorable sensory characteristics of roasted peanuts and tree nuts, such as cashews. Only a handful of AGEs have been characterized, and N(6)-Carboxymethyl lysine (CML) is one of the more commonly used AGE markers in food processing analysis. We evaluated a commercially available anti-CML antibody on raw and roasted cashew extracts. Cashew extracts were separated by SDS-PAGE, transferred to PVDF membrane, immunoblotted with the CML antibody, and bands were visualized by enhanced chemiluminescence. We observed two bands migrating in the range of 10-12kDa that were recognized by the anti-CML antibody. We speculate, based upon their size, that these bands may represent the isoforms of Ana o 3, a 2S albumin allergen. Surprisingly, the signal intensity was the same between raw and roasted cashew extracts, indicating that thermal processing did not induce increased CML reactive modification. This is the first identification of specific protein bands within cashew nuts that carry a CML reactive modification.