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Screening and Optimization of Alkaline Protease Production from Bacteria Isolated from Seawater in The North West of Algeria.

Authors :
Nourine, Zeyneb
Zohra, El Kadi Fatima
Didaoui, Hayat
Kanoun, Khedoudja
Bouchouicha, Sara
Bouyakoub, Nesrine
Benine, Mohamed Lamine
Mouffok, Benali
Harir, Noria
Abbouni, Bouziane
Megharbi, Aicha
Source :
Egyptian Academic Journal of Biological Sciences, C Physiology & Molecular Biology; Jun2023, Vol. 15 Issue 1, p85-96, 12p
Publication Year :
2023

Abstract

Bacteria are attracting the interest of worldwide investors; their use is interesting in several industrial fields, this organism produces a wide variety of extracellular enzymes, including proteases. The objective of this study was to evaluate the production of protease by different bacterial strains isolated from local marine samples collected from the Cap Rousseau beach in the Oran city, northwestern Algeria, 44 bacterial isolates were tested for protease production by cultivating them on skim milk agar medium. The proteolytic activities of all strains were tested using skim milk agar and gelatin agar. Among the 14 isolates that showed a significant hydrolysis diameter, two bacterial strains EC2<subscript>3</subscript> and EC2S<subscript>3</subscript> demonstrated the highest potential for protease production and they were selected for further studies. In addition, the extracellular protease was examined using the fermentation production medium at 30°C for 48h, with a constant agitation of 150 rpm. The enzyme activity was determined under varying conditions of pH, incubation temperature, and salt concentration, using Sigma's Universal Protease Activity Assay. The enzyme from EC2<subscript>3</subscript> strain showed higher activity in all cases than the EC2S<subscript>3</subscript> strain, which indicated that it was the most ideal organism for enzyme production. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
2090083X
Volume :
15
Issue :
1
Database :
Complementary Index
Journal :
Egyptian Academic Journal of Biological Sciences, C Physiology & Molecular Biology
Publication Type :
Academic Journal
Accession number :
163878958
Full Text :
https://doi.org/10.21608/EAJBSC.2023.282301