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Partial purification and characterization of extracellular protease from a halophilic and thermotolerant strain <i>Streptomyces pseudogrisiolus </i>NRC-15

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Title Partial purification and characterization of extracellular protease from a halophilic and thermotolerant strain Streptomyces pseudogrisiolus NRC-15
 
Creator Awad, Hassan M
Mostafa, El-Sayed E
Saad, Moataza M
Selim, Mohsen H
Hassan, Helmy M
 
Subject Streptomyces pseudogrisiolus NRC-15
Thermostable alkaline protease
Purification
Characterization
Commercial application
 
Description 305-311
An alkaline protease was purified from a halophilic
and thermotolerant potent alkaline protease-producing strain Streptomyces pseudogrisiolus
NRC-15 using ammonium sulphate precipitation and Sephadex G-100 column
chromatography. The enzyme was purified to 77.24-folds with a yield of 91.8%
and the specific activity was 112 U/mg of protein. The protease showed a single
band on SDS-PAGE with its molecular mass at 20 kDa and exhibited a maximum
relative activity of 100% using casein as a substrate and. The enzyme had an
optimum pH of 9.5 and displayed optimum activity at 50°C. The enzyme activity
was completely inhibited by the serine protease inhibitor PMSF, suggesting the
presence of serine residue in the active site. The enzyme activity was
increased by the metal ions Ca2+, Co2+, K+ and
Mg2+. The enzyme significantly enhanced the removal of stains when
used with wheel detergent, indicating the potential of the enzyme for using as
a laundry detergent additive to improve the performance of heavy-duty laundry
detergent.
 
Date 2013-09-01T13:16:53Z
2013-09-01T13:16:53Z
2013-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/20880
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.50(4) [August 2013]