In this study, we describe the purification by RP-HPLC and amino acid sequencing by LC-MS of peptides derived from foxtail millet (Setaria italica) meal fermented by Lactobacillus paracasei Fn032. The purified foxtail millet peptide fractions (FFMp) of Tyrosine/Leucine-rich (FFMp4=756.84, FFMp6=678.74 and FFMp10=678.87Da) showed significant (P<0.05) scavenging activities for 1,1-diphenyl-2-picrylhydrazyl (DPPH^•), and superoxide anion (O₂^•−) radicals. FFMp peptides (synthesized) have shown fairly inhibition of the Escherichia coli ATCC 8099 growth. Furthermore, FFMp4 and FFMp6 peptides showed resistance to trypsin proteolysis while FFMp10 appeared to have partial hydrolysis. The results demonstrated that it is feasible to derive natural antioxidants along with antimicrobial activity and resistance to enzyme from fermented foxtail millet meal.