ABSTRACT
Sus scrofa lysozyme (SSL) was digested by different proteases to find peptides with enhanced antibacterial activity against gram-negative bacteria. Hydrolysate with the highest anti-bacterial activity was loaded onto a gel filtration chromatography column followed by a reversed-phase one. The obtained substance was identified by liquid chromatography-mass spectrometry, synthesized to test its antibacterial spectrum and analyzed for bioinformatics. The hydrolysate of trypsin showed the highest antibacterial activity. By purification and identification, the functional peptide with sequence of A-W-V-A-W-K was obtained. The peptide was synthesized and proved to retain partial function of SSL and had activity against gram-negative bacteria. By bioinformatics analysis, the peptide was found to locate in a helix-loop-helix structure, suggesting that the peptide may kill cells by penetrating cell membrane and cause the outflow of cell contents. The discovery of the peptide could lay the foundation for improving the antibacterial activity of SSL.