Identification of antimicrobial peptides of native and heated hydrolysates from hen egg white lysozyme

Hen eggs are a source of bioactive compounds, of which the hen egg white lysozyme (HEWL) protein. HEWL has a demonstrated antibacterial activity. The aim of this study was to evaluate the antimicrobial activity of native and heated HEWL hydrolysates obtained through hydrolysis with pepsin and to identify their peptides using the reversed phase high performance liquid chromatography-electrospray ionization-tandem mass spectrometry (RP-HPLC-ESI-MS-MS) analysis. Native and heat-treated HEWL was hydrolyzed with pepsin at pH 1.2, and their antibacterial activity was tested against Escherichia coli and Staphylococcus carnosus. Two of the hydrolysates obtained presented high antibacterial activity against Gram-positive and Gram-negative bacteria. Native HEWL hydrolysate was a bactericide at 2.0 mg/mL against E. coli. Fifty-one peptide sequences were identified on the two hydrolysates. Peptides identified are cationic peptides. These peptides are rich in Lys and Arg cationic amino acids and have Trp in their sequences.

Bibliographic Details

Main Authors:	Carrillo, W., Ramos, Mercedes
Other Authors:	CSIC-UAM - Instituto de Investigación en Ciencias de la Alimentación (CIAL)
Format:	artículo biblioteca
Language:	English
Published:	Mary Ann Liebert 2018
Subjects:	Antibacterial peptides, Antimicrobial activity, Enzymatic activity, Hydrolysis,
Online Access:	http://hdl.handle.net/10261/192546 http://dx.doi.org/10.13039/501100008351
Tags:	Add Tag No Tags, Be the first to tag this record!