Actinobacteria isolated from Tunisian forest soils show high diversity and biotechnological potential

Actinobacteria are an extremely diverse group of bacteria known for their ability to produce a range of biotechnologically relevant enzymes. Tunisian Forest ecosystems are relatively unexplored in terms of actinobacterial diversity and their enzyme activities, offering an excellent opportunity to is...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biológia 2023-12, Vol.78 (12), p.3653-3665
Hauptverfasser: Hamdi, Chadlia, Arous, Fatma, Boudagga, Soumaya, Harrath, Nouha, Nwodo, Uchechukwu, Jaouani, Atef
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Actinobacteria are an extremely diverse group of bacteria known for their ability to produce a range of biotechnologically relevant enzymes. Tunisian Forest ecosystems are relatively unexplored in terms of actinobacterial diversity and their enzyme activities, offering an excellent opportunity to isolate new potent actinobacterial strains that produce bioactive natural products. In this study, actinobaceria were isolated from soil samples collected from four forests in the Northern part of Tunisia, using Starch-casein media and characterized by morphological, molecular (16 S rRNA) and phenotypic (enzymatic activities) methods. Isolate’s colonies showed a color ranging from whitish, brownish, yellow, green, black, pink-purple and orange, similar to actinobacterial morphology. Analysis of the 16 S rRNA gene sequences of the isolates showed that they belong to the phylum Actinobateria, Specifically the genera Streptomyces , Nocardioides, Arthrobacter, Kocuria and Paenarthrobacter genera with the prevalence of Streptomyces members such as S. albidochromogenes and S. neopeptinius . The analysis of enzymatic profiles, showed that actinobacterial isolates represent a promising source of enzymes with potential biotechnological applications including amylases, CMCase, pectinases, xylanases and laccases.
ISSN:1336-9563
0006-3088
1336-9563
DOI:10.1007/s11756-023-01515-2