title: The lactobin A and amylovorin L471 encoding genes are identical, and their distribution seems to be restricted to the species Lactobacillus amylovorus that is of interest for cereal fermentations.
abstract: Lactobin A and amylovorin L471 are two bacteriocins produced by the phenotypically different strains Lactobacillus amylovorus LMG P-13139 and L. amylovorus DCE 471, respectively. A 110-bp PCR fragment of the structural gene of lactobin A was obtained from total genomic DNA of L. amylovorus LMG P-13139, which was used as a probe to isolate a 3.6-kb HindIII chromosomal fragment for sequencing. PCR amplification revealed that both the structural genes of both the bacteriocins lactobin A and amylovorin L471 were identical. These bacteriocins will be further referred to as amylovorin L. Amylovorin L can be defined as a small, strongly hydrophobic, antibacterial peptide consisting of 50 amino acids. It is synthesized as a precursor peptide of 65 amino acids processed at a characteristic double-glycine proteolytic cleavage site. Amylovorin L hence belongs to the class II bacteriocins. It has a narrow inhibitory spectrum, being most active towards Lactobacillus delbrueckii subsp. bulgaricus LMG 6901(T). Among 38 strains of the Lactobacillus acidophilus DNA homology group, another 6 L. amylovorus strains were also inhibitory towards the L. delbrueckii subsp. bulgaricus LMG 6901(T) strain. The lactobin A or amylovorin L471 structural genes could be detected in the genomes of three of these L. amylovorus strains, but only after extensive PCR amplification, indicating that the inhibitory substances were slightly different. The bacteriocins were characterized as small (approximately 4800 Da), heat-stable peptides that were active in a wide pH range (2.2-8.0). Finally, preliminary experiments indicated that the production of amylovorin L by L. amylovorus DCE 471 took place during a natural rye fermentation, indicating its potential importance in the development of a functional (probiotic) starter culture for cereal fermentations.
authors.affiliation: Research Group of Industrial Microbiology, Fermentation Technology and Downstream Processing, Department of Applied Biological Sciences, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium. ldvuyst@vub.ac.be
authors.forename: L
authors.initials: L
authors.lastname: De Vuyst
authors.forename: L
authors.initials: L
authors.lastname: Avonts
authors.forename: P
authors.initials: P
authors.lastname: Neysens
authors.forename: B
authors.initials: B
authors.lastname: Hoste
authors.forename: M
authors.initials: M
authors.lastname: Vancanneyt
authors.forename: J
authors.initials: J
authors.lastname: Swings
authors.forename: R
authors.initials: R
authors.lastname: Callewaert
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000494:pharmacology; D001430:Bacteriocins / Q000096:biosynthesis / Q000737:chemistry* / Q000494:pharmacology; D001483:Base Sequence; D002523:Edible Grain / Q000382:microbiology*; D005285:Fermentation; D005516:Food Microbiology; D006863:Hydrogen-Ion Concentration; D007779:Lactobacillus acidophilus / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016133:Polymerase Chain Reaction / Q000379:methods; D012689:Sequence Homology, Nucleic Acid
chemical_list: D001426:Bacterial Proteins; D001430:Bacteriocins; C402567:amylovorin L471; C103950:lactobin A protein, Lactobacillus