Exploring the Hot Springs of Golan: A Source of Thermophilic Bacteria and Enzymes with Industrial Promise.
Journal
Current microbiology
ISSN: 1432-0991
Titre abrégé: Curr Microbiol
Pays: United States
ID NLM: 7808448
Informations de publication
Date de publication:
20 Feb 2024
20 Feb 2024
Historique:
received:
20
07
2023
accepted:
14
01
2024
medline:
21
2
2024
pubmed:
20
2
2024
entrez:
20
2
2024
Statut:
epublish
Résumé
In recent years, there has been a surge in research on extremophiles due to their remarkable ability to survive in harsh environments. Extremophile thermophilic bacteria provide thermostable enzymes for biotechnology and industry. Thermophilic bacteria live in extreme environments like hot springs at 45-80 °C. This study screens and isolates thermophilic bacteria and thermozymes from the Golan hot springs in Karakocan, Elazig, Turkey. The study also characterizes thermophilic bacteria and their thermozymes to understand their features and applications better. Golan hot spring water samples at 50 °C yielded 12 isolates. GKE 02, 07, 08, and 10 produce amylase, GKE 04, 08, and 11 cellulase, and GKE 06 xylanase. One isolate (GKE 08) displayed both amylolytic and cellulolytic activity on agar plates. GKE 02 had the highest plate assay amylolytic index (2.3) and amylase activity (67.87 U/ml). Plate assay indicates GKE 08 has 1.5 amylolytic index, 1.1 cellulolytic index, 38.57 U/ml amylase, and 6.81 U/ml cellulase. GKE 04 had the greatest cellulolytic index (1.7) and cellulase activity (27.46). GKE 06, the only xylanase producer, has 19.67 U/ml activity and 1.4 plate assay index. The investigation also included determining the optimal pH and temperature conditions for each enzyme. 16S rDNA gene sequencing revealed seven thermozyme-producing bacteria Bacillus, Geobacillus, and Thermomonas. Thermomonas hydrothermalis genome annotation showed glycosyl hydrolase genes for amylolytic and cellulolytic activity. The findings of this study on thermophilic bacteria and thermostable enzyme synthesis in the Golan hot springs are promising, particularly for T. hydrothermalis, which has limited research on its potential as a thermozyme producer.
Identifiants
pubmed: 38376803
doi: 10.1007/s00284-024-03617-9
pii: 10.1007/s00284-024-03617-9
doi:
Substances chimiques
Amylases
EC 3.2.1.-
Cellulase
EC 3.2.1.4
Water
059QF0KO0R
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
101Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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