Unraveling the enzymatic and antibacterial potential of rare halophilic actinomycetes from Algerian hypersaline wetland ecosystems.


Journal

Journal of basic microbiology
ISSN: 1521-4028
Titre abrégé: J Basic Microbiol
Pays: Germany
ID NLM: 8503885

Informations de publication

Date de publication:
Oct 2022
Historique:
revised: 18 06 2022
received: 12 02 2022
accepted: 10 07 2022
pubmed: 10 8 2022
medline: 5 10 2022
entrez: 9 8 2022
Statut: ppublish

Résumé

The study aimed to isolate rare halophilic actinomycetes from hypersaline soils of Algerian inland Wetland Ecosystems "Sebkhas-Chotts" located in arid and hot hyperarid lands with international importance under the Ramsar Convention and to explore their enzyme-producing and antibacterial abilities. The halophilic actinomycetes were selectively isolated using agar-rich media supplemented with 5, 10, and 15% (W/V) of total salts. Thirty-one isolates were obtained and 16S rRNA gene sequencing analysis revealed the presence of members affiliated to rare halophilic actinobacterial genera (Actinopolyspora and Nocardiopsis) accounting for 74.19% (23 isolates out of 31) and 25.8% (8 isolates), respectively. Both phylotypes are alkalitolerant and halophilic thermotolerant actinomycetes displaying significant hydrolytic activities relative to (amylase, asparaginase, cellulase, esterase, glutaminase, inulinase, protease, pectinase, xylanase), and over 96% of tested isolates exhibited all common enzymes, mainly active at 10% of growing salt. In addition, high antibacterial activity was observed against Bacillus cereus, Bacillus subtilis, Micrococcus luteus, and Staphylococcus aureus. The findings showed that saline wetlands ecosystems represent a rich reservoir for the isolation of significant rare halophilic actinomycetes with potential adaptive features and valuable sources for novel bioactive metabolites and biocatalysts of biotechnological interest.

Identifiants

pubmed: 35945171
doi: 10.1002/jobm.202200085
doi:

Substances chimiques

Anti-Bacterial Agents 0
RNA, Ribosomal, 16S 0
Salts 0
Soil 0
Agar 9002-18-0
Esterases EC 3.1.-
Amylases EC 3.2.1.-
Cellulases EC 3.2.1.-
Polygalacturonase EC 3.2.1.15
Peptide Hydrolases EC 3.4.-
Asparaginase EC 3.5.1.1
Glutaminase EC 3.5.1.2

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1202-1215

Informations de copyright

© 2022 Wiley-VCH GmbH.

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Auteurs

Taha Menasria (T)

Department of Applied Biology, Faculty of Exact Sciences and Natural and Life Sciences, University of Larbi Tebessi, Tebessa, Algeria.
Department of Microbiology, Faculty of Pharmacy, University of Granada, Granada, Spain.

Mercedes Monteoliva-Sánchez (M)

Department of Microbiology, Faculty of Pharmacy, University of Granada, Granada, Spain.

Mabrouka Benhadj (M)

Department of Applied Biology, Faculty of Exact Sciences and Natural and Life Sciences, University of Larbi Tebessi, Tebessa, Algeria.

Leyla Benammar (L)

Department of Microbiology and Biochemistry, Faculty of Natural and Life Sciences University of Batna, Batna, Algeria.

Mourad Boukoucha (M)

Department of Applied Biology, Faculty of Exact Sciences and Natural and Life Sciences, University of Larbi Tebessi, Tebessa, Algeria.

Margarita Aguilera (M)

Department of Microbiology, Faculty of Pharmacy, University of Granada, Granada, Spain.

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