Evidence map›Paper›PMID 41254457›Full record

ArticleProbiotics and antimicrobial proteins2026

Bile Salt Hydrolase Activity in the Food-Derived Strain Levilactobacillus brevis M3R3: Genomic and Functional Characterization.

Gianluigi Agolino, Marianna Cristofolini, Maria Anna Ronsivalle, Alice Cattivelli, Davide Tagliazucchi, Cinzia Caggia, Lisa Solieri, Cinzia L Randazzo

Abstract read
In one paragraph

Article in Probiotics and antimicrobial proteins, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Gianluigi Agolino *Department of Agricultural, Food and Environment, University of Catania, 100, 95123, Catania, Italy.
Marianna Cristofolini *Department of Life Sciences, University of Modena and Reggio Emilia, Besta Building, Via Amendola 2, 42122, Reggio Emilia, Italy.
Maria Anna RonsivalleDepartment of Life Sciences, University of Modena and Reggio Emilia, Besta Building, Via Amendola 2, 42122, Reggio Emilia, Italy.
Alice CattivelliDepartment of Life Sciences, University of Modena and Reggio Emilia, Besta Building, Via Amendola 2, 42122, Reggio Emilia, Italy.
Davide TagliazucchiDepartment of Life Sciences, University of Modena and Reggio Emilia, Besta Building, Via Amendola 2, 42122, Reggio Emilia, Italy.
Cinzia CaggiaDepartment of Agricultural, Food and Environment, University of Catania, 100, 95123, Catania, Italy.
Lisa SolieriDepartment of Life Sciences, University of Modena and Reggio Emilia, Besta Building, Via Amendola 2, 42122, Reggio Emilia, Italy. lisa.solieri@unimore.it.
Cinzia L RandazzoDepartment of Agricultural, Food and Environment, University of Catania, 100, 95123, Catania, Italy.

Funding

Department of Life Sciences, University of Modena and Reggio Emilia FAR2024_PDNextGenerationEU E93C22001090001
6 · The paper itself

Abstract

In the present study, Levilactobacillus brevis M3R3, isolated from traditional Sicilian sourdough, was evaluated for bile salt hydrolase (BSH) activity through kinetic growth assays and bile salts (BSs) deconjugation analysis by UHPLC/HR-MS. Genome sequencing and in silico analyses were performed to assess its safety and probiotic potential. Results showed that strain M3R3 tolerated different concentrations of individual conjugated BSs, with dose-dependent growth inhibition. Exposure to 1.0% glycocholic and glycodeoxycholic acids reduced M3R3 growth, indicating an adaptive stress response. When exposed to a mixed BS solution mimicking intestinal conditions, the strain maintained growth despite an extended lag phase and a reduced final biomass, likely due to toxic BSs accumulation. UHPLC/HR-MS confirmed complete deconjugation of glyco-conjugated BSs and partial deconjugation of tauro-conjugated BSs. Whole-genome sequencing (2.30 Mbp, 2375 CDSs) revealed absence of antimicrobial resistance or virulence genes and identified two bsh genes (bsh_2A and bsh_3A), both expressed under control and BS-exposed conditions. Phylogenetic analysis of L. brevis BSH proteins identified three clusters (I, II, and III), with bsh_2A and bsh_3A from M3R3 grouped in clusters II and III, respectively. Overall, genomic and functional characterizations support that L. brevis M3R3 is a safe, BSH-active strain, with potential applications as a functional ingredient in health promoting formulations.

Indexed as

AmidohydrolasesBacterial ProteinsLevilactobacillus brevisBile Acids and SaltsGenome, BacterialAmidohydrolasesBacterial ProteinsBile Acids and Saltscholoylglycine hydrolaseBile salt hydrolasebsh genesGlyco-conjugated BSsWhole genome

Identifiers

PMID41254457
PMCPMC13342217

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.