“…argued that all possible vulnerable phosphate sites from ovalbumin were merely located on serine 221, 269, and 281 residues and tyrosine 281 under wet‐heating conditions (Sheng et al., 2019). They further pointed out phosphorylation rendered ovalbumin molecular to become more flexible and disordered, which is consistent with the research conducted by other researchers (Sheng et al., 2019; Tang et al., 2019). Considering protein functionalities, such as solubility, thermal stability, apparent viscosity, emulsification, and foaming properties, the hydrophilic phosphorylation of a protein resulted in a distinct enhancement in such intriguing properties (Hao et al., 2019; Sheng et al., 2019; Tang et al., 2019; Wang et al., 2019; Xiong et al., 2016; Yang et al., 2019).…”