MALDI-TOF-MS and in-depth dynamic simulations on the molecular forces determining the stability of the 4-hydroxybenzoic acid - β-Casein complex following UHT-like treatment.

Previous work has suggested the ability of 4-hydroxybenzoic acid (4HBA) to bind to β -casein following ultra high temperature-like processing (UHT) in model aqueous systems. The present work confirmed directly, using MALDI-TOF-MS, the presence of covalently bound 4HBA following UHT-like treatment. In subsequent molecular dynamics simulations, the 3D structure of the β -casein molecule was modified so that the meta-C of 4HBA ring and the side chain amino group of lys32 were linked covalently.