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Production and physicochemical characterization of acidocin D20079, a bacteriocin produced by Lactobacillus acidophilus DSM 20079

Deraz, Sahar LU ; Hedström, Martin LU ; Nordberg Karlsson, Eva LU ; Linse, Sara LU ; Khalil, Ashraf A. and Mattiasson, Bo LU (2007) In World Journal of Microbiology & Biotechnology 23(7). p.911-921
Abstract
Lactobacillus acidophilus DSM 20079 is the producer of a novel bacteriocin termed acidocin D20079. In this paper, a partial sequence of this peptide is determined, together with data on its secondary structure. A modification of the MRS-growth medium (replacing the detergent Tween 80 with oleic acid), was shown to improve the production level of the peptide by one order of magnitude, as well as to stabilize the activity level. Addition of a detergent (Tween 20, less interfering in mass spectrometric analysis), was however necessary for solubilization of the purified acidocin D20079. Digestion of the peptide followed by de-novo sequencing of generated fragments, allowed determination of a partial sequence consisting of 39 of the totally... (More)
Lactobacillus acidophilus DSM 20079 is the producer of a novel bacteriocin termed acidocin D20079. In this paper, a partial sequence of this peptide is determined, together with data on its secondary structure. A modification of the MRS-growth medium (replacing the detergent Tween 80 with oleic acid), was shown to improve the production level of the peptide by one order of magnitude, as well as to stabilize the activity level. Addition of a detergent (Tween 20, less interfering in mass spectrometric analysis), was however necessary for solubilization of the purified acidocin D20079. Digestion of the peptide followed by de-novo sequencing of generated fragments, allowed determination of a partial sequence consisting of 39 of the totally estimated 65 residues. Acidocin D20079 has a high content of glycine residues, hydrophobic residues, and acidic residues. No modified amino acids were found. Edman degradation, and C-terminal sequencing failed, suggesting that the peptide may be cyclic, and a novel member of class IIc bacteriocins. Circular dichroism spectroscopy and secondary structure prediction showed random coil conformation in aqueous solution, but secondary structure was induced in the presence of sodium-dodecyl sulfate. The data could be fitted assuming 2-13% of the residues to be in alpha-helix and 23-27% of the residues to be in beta-strand conformation. This indicates that a membrane/membrane-mimicking hydrocarbon-water interface induces an active conformation. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
inhibitory activity, antimicrobial protein, Lactobacillus, acidocin D20079, bacteriocin, bacteriocin purification
in
World Journal of Microbiology & Biotechnology
volume
23
issue
7
pages
911 - 921
publisher
Springer
external identifiers
  • wos:000247392800003
  • scopus:34249812397
ISSN
0959-3993
DOI
10.1007/s11274-006-9314-2
language
English
LU publication?
yes
id
9206c02a-e2cb-4f1f-93e7-a449da6bc8e3 (old id 648217)
date added to LUP
2007-12-11 11:34:35
date last changed
2017-01-01 06:42:57
@article{9206c02a-e2cb-4f1f-93e7-a449da6bc8e3,
  abstract     = {Lactobacillus acidophilus DSM 20079 is the producer of a novel bacteriocin termed acidocin D20079. In this paper, a partial sequence of this peptide is determined, together with data on its secondary structure. A modification of the MRS-growth medium (replacing the detergent Tween 80 with oleic acid), was shown to improve the production level of the peptide by one order of magnitude, as well as to stabilize the activity level. Addition of a detergent (Tween 20, less interfering in mass spectrometric analysis), was however necessary for solubilization of the purified acidocin D20079. Digestion of the peptide followed by de-novo sequencing of generated fragments, allowed determination of a partial sequence consisting of 39 of the totally estimated 65 residues. Acidocin D20079 has a high content of glycine residues, hydrophobic residues, and acidic residues. No modified amino acids were found. Edman degradation, and C-terminal sequencing failed, suggesting that the peptide may be cyclic, and a novel member of class IIc bacteriocins. Circular dichroism spectroscopy and secondary structure prediction showed random coil conformation in aqueous solution, but secondary structure was induced in the presence of sodium-dodecyl sulfate. The data could be fitted assuming 2-13% of the residues to be in alpha-helix and 23-27% of the residues to be in beta-strand conformation. This indicates that a membrane/membrane-mimicking hydrocarbon-water interface induces an active conformation.},
  author       = {Deraz, Sahar and Hedström, Martin and Nordberg Karlsson, Eva and Linse, Sara and Khalil, Ashraf A. and Mattiasson, Bo},
  issn         = {0959-3993},
  keyword      = {inhibitory activity,antimicrobial protein,Lactobacillus,acidocin D20079,bacteriocin,bacteriocin purification},
  language     = {eng},
  number       = {7},
  pages        = {911--921},
  publisher    = {Springer},
  series       = {World Journal of Microbiology & Biotechnology},
  title        = {Production and physicochemical characterization of acidocin D20079, a bacteriocin produced by Lactobacillus acidophilus DSM 20079},
  url          = {http://dx.doi.org/10.1007/s11274-006-9314-2},
  volume       = {23},
  year         = {2007},
}