ArticleMicroorganisms2018
Production and Characterization of an Extracellular Acid Protease from Thermophilic Brevibacillus sp. OA30 Isolated from an Algerian Hot Spring.
Article in Microorganisms, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- Valorization of protein-rich waste for industrial enzyme production: Purification and cheese making performance of a novel milk clotting protease from Streptomyces thermolineatus GZ1B10.World journal of microbiology & biotechnology · 2026Article
- Characterization, whole-genome sequence analysis, and protease production of a new thermophilic Bacillus licheniformis strain isolated from Debagh hot spring, Algeria.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Potential of the Liquid Fermentation of Fishery Waste byPolymers · 2022Article
- Multidisciplinary involvement and potential of thermophiles.Folia microbiologica · 2019Review
- Editorial for the Special Issue: Thermophiles and Thermozymes.Microorganisms · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases have numerous biotechnological applications and the bioprospection for newly-thermostable proteases from the great biodiversity of thermophilic microorganisms inhabiting hot environments, such as geothermal sources, aims to discover more effective enzymes for processes at higher temperatures. We report in this paper the production and the characterization of a purified acid protease from strain OA30, a moderate thermophilic bacterium isolated from an Algerian hot spring. Phenotypic and genotypic study of strain OA30 was followed by the production of the extracellular protease in a physiologically-optimized medium. Strain OA30 showed multiple extracellular proteolytic enzymes and protease 32-F38 was purified by chromatographic methods and its biochemical characteristics were studied. Strain OA30 was affiliated with
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