Acetylation was performed in conditions similar to a physiologic cell in order to be er understand the acetylation potential in a se ing inside the body. The acetylation of β-Conglycinin was characterized by the analysis of its absorbance and fluorescence properties, as well as through mass spectroscopy. UV-Vis spectroscopy provided insights into chemical modifications occurring in the protein. A peak was observed around 275nm, where acetylation of lysine residues may introduce new chromophores or alter the electronic environment of nearby aromatic residues, leading to changes in the UV-Vis spectrum. The observed peak could thus arise from a combination of aromatic residues and acetylated lysines. Fluorescence spectroscopy was also employed to assess alterations in the intrinsic fluorescence properties of β-conglycinin post-acetylation. A notable decrease in fluorescence in the acetylated compared to the regular protein occurred which likely reflects changes in protein conformation, chemical environment, and interactions induced by acetylation. A change in fluorescence is expected as lysine acetylation may result in fluorescence quenching, reducing the emission intensity. The addition of acetyl groups can introduce electron-withdrawing properties, which can affect the fluorescence of nearby chromophores. Further spectroscopy studies are required to determine the nature of the reduction in fluorescence. Mass spectrometry served as an effective tool for the analysis of the acetylated protein and confirmed the presence of acetyl groups. Acetylated peptides would exhibit a mass shift corresponding to the addition of an acetyl group (42.0106 Da) to lysine residues, where this shift was detected, identifying the presence of acetylated proteins within the sample. Mass spectrometry validated the successful modification of β-conglycinin.