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Open AccessArticle

Production and Characterization of an Extracellular Acid Protease from Thermophilic Brevibacillus sp. OA30 Isolated from an Algerian Hot Spring

1
Equipe Métabolites des Extrêmophiles, Laboratoire de Recherche Biotechnologie et Qualité des Aliments (BIOQUAL), Institut de la Nutrition, de l’Alimentation et des Technologies Agro Alimentaires (INATAA), Université Frères Mentouri Constantine 1 (UFMC1), Route de Ain El Bey, 25000 Constantine, Algérie
2
Grupo EXPRELA, Centro de Investigacións Científicas Avanzadas (CICA), Facultade de Ciencias, Universidade da Coruña, 15071 A Coruña, Spain
3
Laboratoire Alimentation, Nutrition et Santé (ALNUTS), Institut de la Nutrition, de l’Alimentation et des Technologies Agro Alimentaires (INATAA), Université Frères Mentouri Constantine 1 (UFMC1), Route de Ain El Bey, 25000 Constantine, Algérie
*
Author to whom correspondence should be addressed.
Microorganisms 2018, 6(2), 31; https://doi.org/10.3390/microorganisms6020031
Received: 14 March 2018 / Revised: 10 April 2018 / Accepted: 10 April 2018 / Published: 12 April 2018
(This article belongs to the Special Issue Thermophiles and Thermozymes)
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 Brevibacillus thermoruber species. Protease 32-F38 had an estimated molecular weight of 64.6 kDa and was optimally active at 50 °C. It showed a great thermostability after 240 min and its optimum pH was 6.0. Protease 32-F38 was highly stable in the presence of different detergents and solvents and was inhibited by metalloprotease inhibitors. The results of this work suggest that protease 32-F38 might have interesting biotechnological applications. View Full-Text
Keywords: Brevibacillus sp. OA30; thermophilic; hot spring; Algeria; protease; characterization Brevibacillus sp. OA30; thermophilic; hot spring; Algeria; protease; characterization
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Gomri, M.A.; Rico-Díaz, A.; Escuder-Rodríguez, J.-J.; El Moulouk Khaldi, T.; González-Siso, M.-I.; Kharroub, K. Production and Characterization of an Extracellular Acid Protease from Thermophilic Brevibacillus sp. OA30 Isolated from an Algerian Hot Spring. Microorganisms 2018, 6, 31.

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