A thermophilic bacterium, designated Geobacillus sp. Geo 8.1, was isolated from a submarine hydrothermal spring of Ischia Island (Italy) and characterized through genomic and biochemical analyses to evaluate its biotechnological potential. The draft genome (3.41 Mbp; GC 52.5%) revealed 3,751 coding sequences, including complete pathways for carbohydrate, lipid, and protein metabolism, and enzymes involved in stress response and hydrocarbon degradation. Phylogenomic and digital DNA-DNA hybridization analyses placed Geo 8.1 within the Geobacillus thermoleovorans/Geobacillus kaustophilus cluster. Functional annotation highlighted diverse genes encoding thermostable hydrolases such as xylanases, beta-xylosidases, lipases, proteases, and alpha-amylases, together with catalases and dehalogenases relevant to environmental and industrial applications. Crude enzyme extracts exhibited strong xylanase activity (184 U/mL at 65 degrees C), and thin-layer chromatography confirmed the production of xylose as the major hydrolysis product, indicating the coordinated action of endo-xylanase and beta-xylosidase. Genome reconstruction further demonstrated a complete D-xylose utilization pathway linking hemicellulose degradation to central carbon metabolism. The combined genomic and enzyme data reveal Geobacillus sp. Geo 8.1 represents a promising thermophilic biocatalyst for producing thermostable enzymes applicable to lignocellulose valorization, bioremediation, and various industrial processes.

Genomic and functional insights into the thermophilic strain Geobacillus sp. Geo 8.1: a source of thermostable xylanase for sustainable bioprocesses

Finore I.
;
Leone L.;Poli A.;
2026

Abstract

A thermophilic bacterium, designated Geobacillus sp. Geo 8.1, was isolated from a submarine hydrothermal spring of Ischia Island (Italy) and characterized through genomic and biochemical analyses to evaluate its biotechnological potential. The draft genome (3.41 Mbp; GC 52.5%) revealed 3,751 coding sequences, including complete pathways for carbohydrate, lipid, and protein metabolism, and enzymes involved in stress response and hydrocarbon degradation. Phylogenomic and digital DNA-DNA hybridization analyses placed Geo 8.1 within the Geobacillus thermoleovorans/Geobacillus kaustophilus cluster. Functional annotation highlighted diverse genes encoding thermostable hydrolases such as xylanases, beta-xylosidases, lipases, proteases, and alpha-amylases, together with catalases and dehalogenases relevant to environmental and industrial applications. Crude enzyme extracts exhibited strong xylanase activity (184 U/mL at 65 degrees C), and thin-layer chromatography confirmed the production of xylose as the major hydrolysis product, indicating the coordinated action of endo-xylanase and beta-xylosidase. Genome reconstruction further demonstrated a complete D-xylose utilization pathway linking hemicellulose degradation to central carbon metabolism. The combined genomic and enzyme data reveal Geobacillus sp. Geo 8.1 represents a promising thermophilic biocatalyst for producing thermostable enzymes applicable to lignocellulose valorization, bioremediation, and various industrial processes.
2026
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
Geobacillus
Biotechnological potential
Genome analysis
Submarine hydrothermal spring (Ischia island)
Thermophiles
Thermostable enzymes
Xylan degradation
Xylanase
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/574663
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