Abstract

This study compares the efficiency of weak acid hydrolysis (WAH) using formic acid (FA) and hydrochloric acid (HCl) in the analysis of myoglobin peptides. WAH using 2% and 5% formic acid resulted in the identification of 32 peptides, with varying degrees of cleavage at the C-terminus of aspartic acid residues. HCl WAH with different concentrations demon- strated an increase in the total number of identified peptides but a decrease in fully cleaved peptides as the HCl concentration increased. Notably, deamidation was observed during HCl WAH but not in FA WAH. The addition of HCl WAH after FA WAH provided a similar pattern to HCl WAH, with slightly higher levels of hydrolysis. These findings highlight distinct cleavage pat- terns and deamidation effects between FA and HCl in the context of WAH.