A　new　type　of　zinc-chelating　peptide　was　fabricated　from　Octopus　scraps　protein　hydrolysate　and　its　antibacterial　activity　against　Staphylococcus　aureus　was　characterized.　Results　of　Fluorescence　spectra　and　Fourier　Transform　Infrared　Spectrometer　(FT-IR)　demonstrated　that　the　amino　nitrogen　atoms　and　the　oxygen　atoms　belonging　to　the　carboxylate　groups　were　the　primary　chelating　sites　for　zinc　ions.　The　zinc-peptide　chelate　exerted　remarkably　antimicrobial　ability　towards　S.　aureus,　whose　minimum　inhibitory　concentration　(MIC)　was　1.56　mg/mL.　To　investigate　the　antibacterial　mechanism,　changes　of　bacterial　morphology,　cell　constituents,　membrane　potential,　intracellular　reactive　oxygen　species　(ROS)　level　and　intracellular　enzyme　activity　were　measured.　Results　revealed　that　Zn-peptide　exerted　its　bactericidal　activity　by　damaging　bacterial　cell　membranes　and　cell　walls,　increasing　the　cell　permeability　which　resulted　in　structural　lesions　and　release　of　cell　components.　Besides,　Zn-peptide　induced　S.　aureus　cell　death　via　ROS　triggered　pathway.　These　findings　further　promote　the　development　of　Zn-peptide　complexes,　suggesting　that　Zn-peptide　chelate　has　potential　as　natural　bacteriostatic　agent　in　food　processing　industry.