Identification and Functional Analysis of Novel SNPs in Enterocin Genes of Enterococcus faecium GHB21.

This study investigates the functional and structural impact of single nucleotide polymorphisms (SNPs) in the enterocin and associated immunity genes of Enterococcus faecium GHB21, a strain known for producing potent antimicrobial peptides. Enterocins, most of them classified as class IIa bacteriocins, exhibit strong activity against pathogens such as Listeria monocytogenes, making them promising candidates for food preservation and therapeutic interventions. Using cloning, sequencing, and bioinformatics tools, we analyzed key enterocin genes (entA, entB and entP) and their associated immunity genes (entAi and entPi).

Effect Oral Administration Ampicillin on the Ecological Balance of rat Enterococcal gut Microbiota.

The main objective of this work is to investigate the impact of oral administration of ampicillin on the ecological balance of enterococci in the intestinal microbiota of rats during a treatment and a post-treatment. The results have showed that the treated animals excreted significantly higher percentages of resistant enterococci compared to the control group (P ≤ 0.05) during the treatment and after the treatment.

Screening of the Enterocin-Encoding Genes and Their Genetic Determinism in the Bacteriocinogenic Enterococcus faecium GHB21.

Enterococci are well-known for their ability to produce a variety of antimicrobial peptides called enterocins. Most of these enterocins withstand extreme conditions and are very effective against a broad spectrum of undesirable bacteria including some Gram-negative bacteria. The same enterococci strain can produce multiple enterocins simultaneously.

Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity.

Casein from ovine and bovine milk were hydrolyzed with two extracellular protease preparations from Lactobacillus brevis and Lactococcus lactis. The hydrolysates were analyzed by HPLC-MS/MS for peptide identification. A strain-dependent peptide profile could be observed, regardless of the casein origin, and the specificity of these two proteases could be computationally ascribed.