Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14.
Abstract: A novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14 isolated from a horse's intestinal tract was identified. Lacticin Z was purified through a three step procedure comprised of hydrophobic-interaction, cation-exchange chromatography, and reverse-phase HPLC. ESI-TOF MS determined the molecular mass of lacticin Z to be 5,968.9 Da. The primary structure of lacticin Z was found to consist of 53 amino acid residues without any leader sequence or signal peptide. Lacticin Z showed homology to lacticin Q from L. lactis QU 5, aureocin A53 from Staphylococcus aureus A53, and mutacin BHT-B from Streptococcus rattus strain BHT. It exhibited a nanomolar range of MICs against various Gram-positive bacteria, and the activity was completely stable up to 100 degrees C. Unlike many of other LAB bacteriocins, the stability of lacticin Z was emphasized under alkaline conditions rather than acidic conditions. All the results indicated that lacticin Z belongs to a novel type of bacteriocin.
Publication Date: 2007-08-07 PubMed ID: 17690480DOI: 10.1271/bbb.70169Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research focuses on the discovery and analysis of a new bacterial toxin, lacticin Z, produced by a strain of bacteria found in a horse’s intestinal tract. This toxin effectively kills various strains of gram-positive bacteria and maintains stability even under high heat and alkaline conditions.
Isolation and Purification of Lacticin Z
- The bacterium Lactococcus lactis QU 14, which produces lacticin Z, was isolated from a horse’s intestines.
- To extract and purify lacticin Z, a multi-step process involving hydrophobic-interaction, cation-exchange chromatography, and reverse-phase HPLC was used.
Molecular Characteristics of Lacticin Z
- Using ESI-TOF MS, the team was able to determine the molecular mass of lacticin Z to be 5,968.9 Da.
- Lacticin Z was found to be made up of 53 amino acid residues and does not have any leader sequence or signal peptide often found in other proteins.
- Homology, or similar characteristics, was found between lacticin Z and other bacteriocins such as lacticin Q, aureocin A53, and mutacin BHT-B. This implies that lacticin Z might act in a similar fashion or have similar structures to these other bacteriocins.
Antibacterial Activity and Stability of Lacticin Z
- Lacticin Z was found to be effective against various Gram-positive bacteria, as indicated by its nanomolar range of Minimum Inhibitory Concentrations (MICs).
- The bacteriocin was found to be extremely hardy, maintaining complete stability up to a temperature of 100 degrees Centigrade.
- Unlike many bacteriocins from Lactic Acid Bacteria (LAB), lacticin Z remained stable under alkaline conditions rather than acidic ones.
Conclusion
- Based on its unique characteristics, researchers concluded that lacticin Z represents a new type of bacteriocin. This opens up opportunities for its potential use in various applications, particularly those that require conditions of high heat or alkalinity.
Cite This Article
APA
Iwatani S, Zendo T, Yoneyama F, Nakayama J, Sonomoto K.
(2007).
Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14.
Biosci Biotechnol Biochem, 71(8), 1984-1992.
https://doi.org/10.1271/bbb.70169 Publication
Researcher Affiliations
- Laboratory of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Hakozaki, Fukuoka, Japan.
MeSH Terms
- Amino Acid Sequence
- Animals
- Bacterial Proteins
- Bacteriocins / chemistry
- Bacteriocins / isolation & purification
- Bacteriocins / pharmacology
- Chromatography
- Gram-Positive Bacteria / drug effects
- Horses
- Lactococcus lactis / chemistry
- Microbial Sensitivity Tests
- Sequence Homology, Amino Acid
- Spectrometry, Mass, Electrospray Ionization
Citations
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