A novel conformation-dependent monoclonal antibody specific to the native structure of beta-lactoglobulin and its application

Journal of Dairy Science
W L ChenS J T Mao

Abstract

Molten globules are thought to be general intermediates in protein folding and unfolding. beta-lactoglobulin (beta-LG) is one of the major bovine whey proteins, constituting approximately 10 to 15% of total milk proteins. We have recently identified beta-LG as a superior marker for evaluating thermally processed milk. Strand D of beta-LG participates in irreversible thermal unfolding as probed by a monoclonal antibody (mAb) specific to thermally denatured beta-LG. In the present study, we used native beta-LG as an immunogen to test the hypothesis that a specific mAb against the native beta-LG could be established. As result, a mAb (4H11E8) directed against the native structure of beta-LG was made. The antibody did not recognize the heat-denatured form of beta-LG, such as its dimer and aggregates. Immunoassay using this "native" mAb showed that the stability of beta-LG was at temperatures < or =70 degrees C. beta-Lactoglobulin began to deteriorate between 70 and 80 degrees C over time. The denaturation was correlated with the transition temperature of beta-LG. Further chemical modification of Cys (carboxymethylation) or positively charged residues (acetylation) of beta-LG totally abolished its immunoreactivity, confirming the co...Continue Reading

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Citations

Jan 20, 2007·Journal of Dairy Science·H C LiuS J T Mao
Dec 20, 2008·Veterinary Research·I-Hsiang LaiSimon J T Mao
Dec 1, 2012·Annals of the New York Academy of Sciences·Chris HollowayDaan J A Crommelin
Dec 14, 2016·BioMed Research International·Chun San TaiWen Liang Chen
Jun 6, 2009·Journal of Agricultural and Food Chemistry·Asghar Taheri-KafraniThomas Haertle

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