Building on this fundamental understanding, our current study seeks to further evaluate LplA's substrate tolerance, analytical methods, and potential broader applications in the field of bioconjugation. We systematically introduced azido groups into a variety of proteins, followed by the coupling of Cy3, a fluorescent molecule, via click chemistry. The proteins we examined included egg-derived proteins ovalbumin (OVA), ovotransferrin (OVT), egg-derived lysozyme, bovine serum albumin (BSA), human serum albumin (HSA), human lysozyme (hLysozyme), betalactoglobulin (BLG), and transferrin. The success of the modification varied from each of the proteins, with the results confirmed by both SDS-PAGE and RP-HPLC analysis optimized by BioResolve RP mAb polyphenyl column . The Solvent Accessible Surface Area (SASA) of these proteins was then examined to reveal the correlation between SASA values and the feasibility of modification. These results contribute to the evolving understanding of the potential of LplA as a versatile tool in bioconjugation and set the stage for future research endeavors.