For each group, 3 mL of culture supernatant was collected in biological triplicates. The supernatants were then centrifuged at 3,000 xg to remove cell debris and filtered through a 0.22um filter. The filtered supernatants were immediately supplemented with a protease inhibitor cocktail (EDTA-free) to prevent degradation of secreted proteins. Protein concentration was performed using centrifugal ultrafiltration units with a molecular weight cut-off (MWCO) of 3 kDa or 10 kDa. Subsequently, four volumes of ice-cold acetone were added to the samples to precipitate the proteins. Protein samples were subjected to SDS-PAGE followed by silver staining to assess sample quality. Upon confirmation of adequate protein quality, the extracted proteins were digested using enzymes to generate peptides.