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The objectives of this study were to isolate and purify the natural antimicrobial peptide from Munggae, Halocynthia roretzi. First, the crude antimicrobial extracts were obtained by treatment using 5% acetic acid. The antimicrobial activities of the crude extracts were 50% less than that of nisin and 50 times less than that of lysozyme. Their antimicrobial activities also showed great stability even after heat treatment at 100℃ for 10 min. This was followed by gel permeation chromatography (GPC), preparative acid urea - polyacrylamide gel electrophoresis (Prep. AU-PAGE) and reversed phase - high performance liquid chromatography (RP-HPLC). The purified peptide showed strong antimicrobial activity against E. coli. Through the purification processes, the peptide's antimicrobial activity increased 200 times more than the initial crude extract. As a result of tricine SDS-PAGE, the peptide was about 5.5 kDa molecular mass and existed as a monomer without disulfide bond. Therefore, the antimicrobial activities of Munggae extracts were mainly due to the antimicrobial peptides less than 10 kDa molecular mass.