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  4. Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization
 
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Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization

Publikationstyp
Journal Article
Date Issued
2015-07-10
Sprache
English
Author(s)
Ibrahim, Abdelnasser S. S.  
Al-Salamah, Ali A.  
El-Badawi, Yahya B.  
El-Tayeb, Mohamed A.  
Antranikian, Garabed  
Institut
Technische Mikrobiologie V-7  
TORE-URI
http://hdl.handle.net/11420/6632
Journal
Extremophiles  
Volume
19
Issue
5
Start Page
961
End Page
971
Citation
Extremophiles 5 (19): 961-971 (2015)
Publisher DOI
10.1007/s00792-015-0771-0
Scopus ID
2-s2.0-84940185880
Publisher
Springer
Alkaline protease produced by the halotolerant alkaliphilic Bacillus sp. strain NPST-AK15 was purified to homogeneity by the combination of ammonium sulfate precipitation, anion-exchange and gel permeation chromatography. The purified enzyme was a monomeric protein with an estimated molecular weight of 32 kDa. NPST-AK15 protease was highly active and stable over a wide pH range, with a maximal activity at pH 10.5. The enzyme showed optimum activity at 60 °C and was stable at 30–50 °C for at least 1 h. Thermal stability of the purified protease was substantially improved by CaCl2 (1.1- to 6.6-fold). The Km, Vmax and kcat values for the enzyme were 2.5 mg ml−1, 42.5 µM min−1 mg−1, and 392.46 × 103 min−1, respectively. NPST-AK15 protease activity was strongly inhibited by PMSF, suggesting that the enzyme is a serine protease. The enzyme was highly stable in NaCl up to 20 % (w/v). Moreover, the purified enzyme was stable in several organic solvents such as diethyl ether, benzene, toluene, and chloroform. In addition, it showed high stability and compatibility with a wide range of surfactants and commercial detergents and was slightly activated by hydrogen peroxide. These features of NPST-AK15 protease make this enzyme a promising candidate for application in the laundry and pharmaceutical industries.
Subjects
alkaline protease
alkaliphiles
bacillus sp
detergent stable
purification
solvent stable
DDC Class
570: Biowissenschaften, Biologie
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