Egg white proteins are susceptible to heat treatment and form aggregates that are unfavorable for food pro-
cessing, leading to efficiency and quality problems. This study aims to improve the thermal stability of egg white
proteins (mainly ovalbumin, OVA) in the food industry. These study procedures included the alkaline heat
treatment for the preparation of S-ovalbumin (S-OVA) and the modification with positively charged amino acids
amino acids. These processes were aimed at studying the transformation of the S-configuration and the inhibition
mechanism of heat-induced aggregation by positively charged amino acid modification. The results indicate that
the interactions between arginine, histidine (His) and lysine (Lys) with OVA are characterized by the presence of
hydrogen bonding and hydrophobic interactions in addition to potential electrostatic interactions. His, in
particular, exhibits unique binding behaviors and sites due to the additional hydrophobic interactions of its
imidazole ring, albeit at a comparative disadvantage in terms of electrostatic interactions. The mechanism for
enhanced thermal stability via the transformation of the S-configuration primarily involves the suppression of
disulfide bond formation. Conversely, the role of amino acid modification in reducing the formation of protein
aggregates is attributed to the reduction of non-covalent interactions between proteins. This study elucidates the
specific mechanisms by which S-configuration transformation and amino acid modification enhance the thermal
stability of OVA, providing a novel approach to augment the thermal processing capabilities of egg white.