Volume 6, Issue 1 (2015)
JMBS 2015, 6(1): 50-60 |
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Badoei-dalfard A. Isolation and biochemical characterization of detergent stable protease from Bacillus pumilus. JMBS 2015; 6 (1) :50-60
URL: http://biot.modares.ac.ir/article-22-4436-en.html
URL: http://biot.modares.ac.ir/article-22-4436-en.html
Abstract: (11756 Views)
In this study, a Bacillus species was identified from the Dosarri mineral spring in Jiroft microflora. This strain produce clear halo in casein agar media. It has been identified as Bacillus Pumilus (KHB3) based on biochemical tests and 16S rRNA gene sequencing. To enzyme production, this strain was cultured in specific medium for 48 h. Supernatant was partially purified after precipitation with ammonium sulphate (85 %), dialysis and ion exchange chromatography (Q-Sepharose). KHB3 protease was characterized in the presence of different pHs, ions and detergents. Results indicated that the enzyme showed maximum activity and stability in pH 8.0. This enzyme retained about 100 % of its activity in the presence of 1.0 and 1.5 M NaCl. KHB3 protease showed 33 and 10 % increase in protease activity in the presence of MnSO4 and FeSO4. KHB3 protease retained at least 45 % of its activity and stability in the presence of commercial detergents. In addition, it show 12 % increase in enzyme activity in the presence of Banoo detergent. Activity and stability in alkaline pH, organic solvents and detergent compounds show that this protease has high value capacity in detergent industry.
Article Type: _ |
Subject:
biochemistry
Received: 2015/03/5 | Accepted: 2015/09/23 | Published: 2015/10/13
Received: 2015/03/5 | Accepted: 2015/09/23 | Published: 2015/10/13
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