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Effect of processing on the detectability of peanut protein by ELISA.

Posted by on in 2013
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Iqbal A1Ateeq N. 2013. Food Chem. 2013. 141:1651-4. doi: 10.1016/j.foodchem.2013.04.102. Epub 2013 May 10.

1Science and Advice for Scottish Agriculture (SASA), Roddinglaw Road, EH12 9FJ Edinburgh, United Kingdom. amjadiqbal147@yahoo.com

Abstract

Chicken IgY was used for the detection and quantification of peanut proteins by indirect competitive ELISA. The method was optimized by using a checker board approach to determine the optimal concentration of coating antigen, primary antibody and secondary antibody. Peanut protein could be detected in foods down to levels of 10 ppm. The effect of physical (heat treatment at 80 °C and 100 °C) and chemical (acid, alkali and reducing sugar) treatments on the IgY binding of peanut proteins was investigated. The optimized assay was relatively sensitive for the roasted peanut proteins. However, the binding ability of chicken IgYs to peanut proteins was found to be significantly altered by denaturation and hydrolysis of proteins. It was also observed that the effect of Millard chemistry on the detectability of peanut protein was less pronounced at high temperatures than at low temperatures.

Copyright © 2013 Elsevier Ltd. All rights reserved.

KEYWORDS:

Allergens, ELISA, Epitopes, Peanut protein, Stability

PMID:
23870873
[PubMed - indexed for MEDLINE]
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