title: Isolation and characterization of an antibacterial peptide fraction from the pepsin hydrolysate of half-fin anchovy (Setipinna taty).
abstract: Enzymatic proteolysis of food proteins is considered a promising method to generate antibacterial peptides. The objective of the present study was to isolate and characterize peptide fraction from the pepsin hydrolysate of half-fin anchovy (Setipinna taty) with antibacterial activity against Escherichia coli. The most active peptide fraction HAHp2-3-I was isolated by a series of chromatographic methods, including Sephadex G-25 chromatography, reverse high-performance liquid chromatography (RP-HPLC) and Source 5RPC ST. Peptides identification of HAHp2-3-I was carried out using UPLC-LTQ-Orbitrap mass spectrometer. HAHp2-3-I contained five cationic peptides (MLTTPPHAKYVLQW, SHAATKAPPKNGNY, PTAGVANALQHA, QLGTHSAQPVPF and VNVDERWRKL) and three anionic peptides (LATVSVGAVELCY, NPEFLASGDHLDNLQ and PEVVYECLHW). Prediction of peptide secondary structure indicated that these anionic peptides should have extended strand and random coil structures, whereas cationic peptides PTAGVANALQHA and VNVDERWRKL could form alpha helixes. In addition, results of scanning electron microscopy (SEM) revealed that treatment by HAHp2-3-I could cause the morphological changes of E. coli and destruction of the cell integrity via irreversible membrane damage. The results could provide information for investigating the antibacterial model of antibacterial peptides derived from fish protein hydrolysates.
authors.affiliation: Department of Food Science, College of Food Science and Pharmacy, Zhejiang Ocean University, Zhoushan 316000, China. rusong@zjou.edu.cn
authors.forename: Ru
authors.initials: R
authors.lastname: Song
authors.forename: Rong-Bian
authors.initials: RB
authors.lastname: Wei
authors.forename: Hong-Yu
authors.initials: HY
authors.lastname: Luo
authors.forename: Dong-Feng
authors.initials: DF
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D056148:Chromatography, Reverse-Phase; D052978:Disk Diffusion Antimicrobial Tests; D004926:Escherichia coli / Q000187:drug effects / Q000648:ultrastructure; D029941:Fish Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D005399:Fishes; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000737:chemistry*; D017433:Protein Structure, Secondary; D059748:Proteolysis; D020539:Sequence Analysis, Protein; D013499:Surface Properties
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D029941:Fish Proteins; D010434:Pepsin A