ArticleInternational microbiology : the official journal of the Spanish Society for Microbiology2025
Purification and characterization of an extremely thermostable metalloprotease from Geobacillus thermoleovorans HBB208.
Article in International microbiology : the official journal of the Spanish Society for Microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- High-level expression and characterization of a thermostable thermolysin-like metalloprotease with industrial potential.Folia microbiologica · 2026Article
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2 authors.
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Abstract
Protease enzymes are widely used in industrial applications, often requiring resistance to alkaline and high-temperature conditions while maintaining activity in organic solvents. Discovering thermotolerant proteases from thermophilic organisms is crucial for such applications. This study aimed to identify a novel thermotolerant protease among 201 thermophilic strains isolated from hot springs in Aydın province. Geobacillus thermoleovorans HBB208 was identified as the most efficient protease producer, exhibiting a 3.1 (D/d) ratio on skim milk agar. The protease purified via ammonium sulfate precipitation, hydrophobic interaction, and ion-exchange chromatography, resulting in a 70.2-fold purification. SDS-PAGE and zymogram analyses confirmed the molecular weight of approximately 33.5 kDa and proteolytic activity. The enzyme showed optimal activity at pH 8.0 and 70 °C, and retained 50% activity after 30 min at 87.3 °C in the presence of 10 mM Ca
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