Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity

Bile salt hydrolase (BSH; EC 3.5.1.24) is the microbial enzyme that catalyzes the conversion of primary bile acids (BAs) into secondary ones, promoting microbial adaptation and modulating several host’s biological functions. Probiotics with BSH activity are supposed to survive harsh intestinal condi...

Full description

Saved in:
Bibliographic Details
Main Authors: Gianluigi Agolino, Marianna Cristofolini, Amanda Vaccalluzzo, Davide Tagliazucchi, Alice Cattivelli, Alessandra Pino, Cinzia Caggia, Lisa Solieri, Cinzia Lucia Randazzo
Format: Article
Language:English
Published: MDPI AG 2025-01-01
Series:Biomolecules
Subjects:
Online Access:https://www.mdpi.com/2218-273X/15/1/86
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1832588916398489600
author Gianluigi Agolino
Marianna Cristofolini
Amanda Vaccalluzzo
Davide Tagliazucchi
Alice Cattivelli
Alessandra Pino
Cinzia Caggia
Lisa Solieri
Cinzia Lucia Randazzo
author_facet Gianluigi Agolino
Marianna Cristofolini
Amanda Vaccalluzzo
Davide Tagliazucchi
Alice Cattivelli
Alessandra Pino
Cinzia Caggia
Lisa Solieri
Cinzia Lucia Randazzo
author_sort Gianluigi Agolino
collection DOAJ
description Bile salt hydrolase (BSH; EC 3.5.1.24) is the microbial enzyme that catalyzes the conversion of primary bile acids (BAs) into secondary ones, promoting microbial adaptation and modulating several host’s biological functions. Probiotics with BSH activity are supposed to survive harsh intestinal conditions and exert a cholesterol-lowering effect. Here, <i>Lacticaseibacillus rhamnosus</i> strains (VB4 and VB1), isolated from the vaginal ecosystem, were submitted to a genomic survey, in vitro BSH activity, and BAs tolerance assay to unravel their probiotic potential as BAs modulators. The draft genomes of <i>Lcb. rhamnosus</i> VB4 and VB1 strains comprised 2769 and 2704 CDSs, respectively. Gene annotation revealed numerous strain-specific genes involved in metabolism and transport, as well as in DNA recombination. Each strain harbors a single <i>bsh</i> gene, encoding a C-N amide hydrolase, which conserved the essential residues required in the BSH core site. According to the results, compared to VB1, the VB4 strain tolerated better BAs stress and was more active in deconjugating BAs. However, BAs stress increased the <i>bsh</i> gene transcription in the VB1 strain but not in the VB4 strain, suggesting a partially nonlinear relationship between BSH activity and gene expression. In conclusion, despite the complexity of the BSH transcriptional system, the results support the VB4 strain as a promising BAs-deconjugating probiotic candidate.
format Article
id doaj-art-93b379660c5348b1a3ce0e8eeb8e0589
institution Kabale University
issn 2218-273X
language English
publishDate 2025-01-01
publisher MDPI AG
record_format Article
series Biomolecules
spelling doaj-art-93b379660c5348b1a3ce0e8eeb8e05892025-01-24T13:25:07ZengMDPI AGBiomolecules2218-273X2025-01-011518610.3390/biom15010086Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase ActivityGianluigi Agolino0Marianna Cristofolini1Amanda Vaccalluzzo2Davide Tagliazucchi3Alice Cattivelli4Alessandra Pino5Cinzia Caggia6Lisa Solieri7Cinzia Lucia Randazzo8Department of Agriculture, Food and Environment, University of Catania, 95123 Catania, ItalyDepartment of Life Science, University of Modena and Reggio Emilia, 42122 Reggio Emilia, ItalyDepartment of Agriculture, Food and Environment, University of Catania, 95123 Catania, ItalyDepartment of Life Science, University of Modena and Reggio Emilia, 42122 Reggio Emilia, ItalyDepartment of Life Science, University of Modena and Reggio Emilia, 42122 Reggio Emilia, ItalyDepartment of Agriculture, Food and Environment, University of Catania, 95123 Catania, ItalyDepartment of Agriculture, Food and Environment, University of Catania, 95123 Catania, ItalyDepartment of Life Science, University of Modena and Reggio Emilia, 42122 Reggio Emilia, ItalyDepartment of Agriculture, Food and Environment, University of Catania, 95123 Catania, ItalyBile salt hydrolase (BSH; EC 3.5.1.24) is the microbial enzyme that catalyzes the conversion of primary bile acids (BAs) into secondary ones, promoting microbial adaptation and modulating several host’s biological functions. Probiotics with BSH activity are supposed to survive harsh intestinal conditions and exert a cholesterol-lowering effect. Here, <i>Lacticaseibacillus rhamnosus</i> strains (VB4 and VB1), isolated from the vaginal ecosystem, were submitted to a genomic survey, in vitro BSH activity, and BAs tolerance assay to unravel their probiotic potential as BAs modulators. The draft genomes of <i>Lcb. rhamnosus</i> VB4 and VB1 strains comprised 2769 and 2704 CDSs, respectively. Gene annotation revealed numerous strain-specific genes involved in metabolism and transport, as well as in DNA recombination. Each strain harbors a single <i>bsh</i> gene, encoding a C-N amide hydrolase, which conserved the essential residues required in the BSH core site. According to the results, compared to VB1, the VB4 strain tolerated better BAs stress and was more active in deconjugating BAs. However, BAs stress increased the <i>bsh</i> gene transcription in the VB1 strain but not in the VB4 strain, suggesting a partially nonlinear relationship between BSH activity and gene expression. In conclusion, despite the complexity of the BSH transcriptional system, the results support the VB4 strain as a promising BAs-deconjugating probiotic candidate.https://www.mdpi.com/2218-273X/15/1/86<i>Lacticaseibacillus rhamnosus</i>bile salt hydrolasebile acids deconjugationprobioticsbile acids stress
spellingShingle Gianluigi Agolino
Marianna Cristofolini
Amanda Vaccalluzzo
Davide Tagliazucchi
Alice Cattivelli
Alessandra Pino
Cinzia Caggia
Lisa Solieri
Cinzia Lucia Randazzo
Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity
Biomolecules
<i>Lacticaseibacillus rhamnosus</i>
bile salt hydrolase
bile acids deconjugation
probiotics
bile acids stress
title Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity
title_full Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity
title_fullStr Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity
title_full_unstemmed Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity
title_short Genome Mining and Characterization of Two Novel <i>Lacticaseibacillus rhamnosus</i> Probiotic Candidates with Bile Salt Hydrolase Activity
title_sort genome mining and characterization of two novel i lacticaseibacillus rhamnosus i probiotic candidates with bile salt hydrolase activity
topic <i>Lacticaseibacillus rhamnosus</i>
bile salt hydrolase
bile acids deconjugation
probiotics
bile acids stress
url https://www.mdpi.com/2218-273X/15/1/86
work_keys_str_mv AT gianluigiagolino genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT mariannacristofolini genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT amandavaccalluzzo genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT davidetagliazucchi genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT alicecattivelli genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT alessandrapino genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT cinziacaggia genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT lisasolieri genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity
AT cinzialuciarandazzo genomeminingandcharacterizationoftwonovelilacticaseibacillusrhamnosusiprobioticcandidateswithbilesalthydrolaseactivity