Identification of antibacterial peptides from ovine α s2-casein

The aim of this work was to isolate and identify antibacterial peptides present in a pepsin digest of ovine α s2-casein. A protein digest with antibacterial properties was first separated by ion exchange chromatography. The fractions most active against Escherichia coli ATCC 25922 were fractionated...

Full description

Saved in:
Bibliographic Details
Published inInternational dairy journal Vol. 16; no. 9; pp. 1072 - 1080
Main Authors López-Expósito, Iván, Gómez-Ruiz, José Ángel, Amigo, Lourdes, Recio, Isidra
Format Journal Article Conference Proceeding
LanguageEnglish
Published Oxford Elsevier Ltd 01.09.2006
Elsevier Science
Subjects
Antibacterial peptide
antibacterial properties
bioactive properties
Biological and medical sciences
casein
Electrospray mass spectrometry
Escherichia coli
ewe milk
Food industries
Food microbiology
fractionation
Fundamental and applied biological sciences. Psychology
human nutrition
in vitro digestion
Milk and cheese industries. Ice creams
Ovine milk
pepsin
peptides
sheep
αs2-Casein
Antibacterial peptide
α s2-Casein
Electrospray mass spectrometry
Ovine milk
Peptides
Dairy product
Identification
Electrospray
Milk protein
Casein
Dairy industry
Antibacterial agent
Mass spectrometry
Milk
αs2-Casein
Online AccessGet full text

Cover

More Information
Summary:The aim of this work was to isolate and identify antibacterial peptides present in a pepsin digest of ovine α s2-casein. A protein digest with antibacterial properties was first separated by ion exchange chromatography. The fractions most active against Escherichia coli ATCC 25922 were fractionated by semi-preparative RP-HPLC, and the identification of the active peptides was carried out by on-line and off-line RP-HPLC-ESI-MS/MS. Following this strategy, 10 different peptides were identified, all corresponding to the C-terminal region of the ovine α s2-casein. Four of them were chemically synthesized and showed antibacterial activity against several Gram-positive and Gram-negative bacteria. Among the synthesized peptides, ovine α s2-casein f(165–181) exhibited the highest antibacterial potency against all bacteria tested. The antimicrobial activity was compared with that of other previously described peptides like lactoferricin and fragment f(183–207) of bovine α s2-casein.
Bibliography:http://dx.doi.org/10.1016/j.idairyj.2005.10.006
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0958-6946
1879-0143
DOI:10.1016/j.idairyj.2005.10.006