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Proteolytic Bacillus sp. Isolation and Identification from Tannery Alkaline Baths

2025-09-05Artigo científico Acesso aberto
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dc.contributor.authorLageiro, Manuela
dc.contributor.authorSimões, Fernanda
dc.contributor.authorAlvarenga, Nuno
dc.contributor.authorReis, Alberto
dc.contributor.institutionGeoBioTec - Geobiociências, Geoengenharias e Geotecnologias
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2025-11-03T21:53:49Z
dc.date.available2025-11-03T21:53:49Z
dc.date.issued2025-09-05
dc.descriptionFunding Information: This research was funded by the Foundation for Science and Technology (FCT) under the grant UIDB/04035/2020 (doi:10.54499/UIDB/04035/2020) to GEOBIOTEC (GeoBioSciences GeoTech-nologies and GeoEngineering) Research Unit. Publisher Copyright: © 2025 by the authors.
dc.description.abstractThe application of microbial alkaline proteases holds significant potential for eco-sustainable industrial processes by reducing chemical usage and lowering the costs of effluent treatment. In the search for novel proteases with industrial relevance, several microbial strains were isolated from alkaline baths of the Portuguese tannery agroindustry. The most promising protease-producing strains were selected for identification and further study. Two isolates demonstrated the highest proteolytic activity, reaching 0.51 ± 0.01 U mL−1 and 0.70 ± 0.01 U mL−1 after 7.5 h of submerged cultivation in nutrient broth. Based on API biochemical tests, molecular biology techniques, and GC-FAME analysis of membrane lipids, the isolates were identified as Bacillus subtilis and incorporated into INIAV’s collection of industrial microbial cultures as B. subtilis CCMI 1253 (BMR2) and B. subtilis CCMI 1254 (BMR1). The most promising protease producer, B. subtilis CCMI 1253 (BMR2), exhibited a maximum specific growth rate of 0.88 ± 0.10 h−1. The proteases produced exhibited good extracellular proteolytic activity, with adaptability to industrial conditions, indicating their suitability for agroindustry applications such as leather making, detergent formulations and the treatment of effluents and protein residues. The results support the potential of microbial proteases as valuable tools in the bioeconomy and green chemistry.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent22
dc.format.extent1845263
dc.identifier.doi10.3390/molecules30173632
dc.identifier.issn1420-3049
dc.identifier.otherPURE: 134810981
dc.identifier.otherPURE UUID: 864d6e7c-c329-400f-9005-6e393ae4cb4b
dc.identifier.otherScopus: 105015895426
dc.identifier.otherPubMed: 40942157
dc.identifier.otherWOS: 001569943100001
dc.identifier.otherPubMedCentral: PMC12430094
dc.identifier.urihttp://hdl.handle.net/10362/190068
dc.identifier.urlhttps://www.scopus.com/pages/publications/105015895426
dc.identifier.urlhttps://www.webofscience.com/wos/woscc/full-record/WOS:001569943100001
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04035%2F2020/PT
dc.relationGeoBioSciences GeoTechnologies and GeoEngineering
dc.subjectBacillus subtilis
dc.subjectBio-economy
dc.subjectDetergent
dc.subjectEnzymatic activity
dc.subjectLeather
dc.subjectProteases
dc.subjectStain removal
dc.subjectAnalytical Chemistry
dc.subjectChemistry (miscellaneous)
dc.subjectMolecular Medicine
dc.subjectPharmaceutical Science
dc.subjectDrug Discovery
dc.subjectPhysical and Theoretical Chemistry
dc.subjectOrganic Chemistry
dc.titleProteolytic Bacillus sp. Isolation and Identification from Tannery Alkaline Bathsen
dc.typejournal article
degois.publication.firstPage1
degois.publication.issue17
degois.publication.lastPage22
degois.publication.titleMolecules
degois.publication.volume30
dspace.entity.typePublication
oaire.awardNumberUIDB/04035/2020
oaire.awardTitleGeoBioSciences GeoTechnologies and GeoEngineering
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04035%2F2020/PT
oaire.fundingStream6817 - DCRRNI ID
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublication79cbe169-6a63-4f2b-a8f3-2b55bb9abfa4
relation.isProjectOfPublication.latestForDiscovery79cbe169-6a63-4f2b-a8f3-2b55bb9abfa4

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