Antimicrobial Peptides Released by Enzymatic Hydrolysis of Hen Egg White Lysozyme

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• 作者：Yoshinori Mine ; Fupeng Ma ; and Sophie Lauriau
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2004
• 出版时间：March 10, 2004
• 年：2004
• 卷：52
• 期：5
• 页码：1088 - 1094
• 全文大小：248K
• 年卷期：v.52,no.5(March 10, 2004)
• ISSN：1520-5118

文摘

This work was aimed at the isolation, purification, and characterization of novel antimicrobial peptidesfrom chicken egg white lysozyme hydrolysate, obtained by peptic digestion and subsequent trypticdigestion. The hydrolysate was composed of over 20 small peptides of less than 1000 Da, and hadno enzymatic activity. The water-soluble peptide mixture showed bacteriostatic activity against Gram-positive bacteria (Staphylococcus aureus 23-394) and Gram-negative bacteria (Escherichia coli K-12).Two bacteriostatic peptides were purified and sequenced. One peptide, with the sequence Ile-Val-Ser-Asp-Gly-Asp-Gly-Met-Asn-Ala-Trp, inhibited Gram-negative bacteria E. coli K-12 and correspondedto amino acid residues 98-108, which are located in the middle part of the helix-loop-helix. Anothernovel antimicrobial peptide inhibited S. aureus 23-394 and was determined to have the sequenceHis-Gly-Leu-Asp-Asn-Tyr-Arg, corresponding to amino acid residues 15-21 of lysozyme. Thesepeptides broadened the antimicrobial activity of lysozyme to include Gram-negative bacteria. Theresults obtained in this study indicate that lysozyme possesses nonenzymatic bacteriostatic domainsin its primary sequence and they are released by proteolytic hydrolysis.Keywords: Egg white lysozyme; lytic activity; bacteriostatic activity; antimicrobial peptides; pepsin;trypsin; SEM; reversed-phase HPLC