Subscribe Now Subscribe Today
Science Alert
 
FOLLOW US:     Facebook     Twitter
Blue
   
Curve Top
Biotechnology
  Year: 2008 | Volume: 7 | Issue: 1 | Page No.: 94-99
DOI: 10.3923/biotech.2008.94.99
Purification and Characterization of Serine Protease from Seeds of Holarrhena antidysenterica
Hidayatullah Khan, M. Subhan, Sultan Mehmood, M. Faran Durrani, Saira Abbas and Sanaullah Khan

Abstract:
Low molecular weight serine protease has been purified from the seeds of Holarrhena antidysenterica to electrophoresis homogeneity by the combination of size exclusion and ion exchange chromatography. The molecular mass was estimated by SDS-PAGE to be about 25 kDa. The enzyme showed optimum activity at pH 7.5 and exhibited its highest activity at 35°C using 1% casein as a substrate. The enzyme was strongly inhibited by 2 mM PMSF but not by EDTA and cysteine protease inhibitors, suggesting the presence of serine residues at the active site. The enzyme had a Km of 1.1 mg mL-1 and Vmax of 389.71 units min-1 mg-1 of protein.
PDF Fulltext XML References Citation Report Citation
 RELATED ARTICLES:
  •    A Mini Review on New Pharmacological and Toxicological Considerations of Protease Inhibitors' Application in Cancer Prevention and Biological Research
  •    Purification and Some Properties of Thermo-stable Alkaline Serine Protease from Thermophilic Bacillus sp. Gs-3
  •    Production and Characterization of Thermo-alkaline Extracellular Protease from Halobacterium sp. AF1
How to cite this article:

Hidayatullah Khan, M. Subhan, Sultan Mehmood, M. Faran Durrani, Saira Abbas and Sanaullah Khan, 2008. Purification and Characterization of Serine Protease from Seeds of Holarrhena antidysenterica. Biotechnology, 7: 94-99.

DOI: 10.3923/biotech.2008.94.99

URL: https://scialert.net/abstract/?doi=biotech.2008.94.99

 
COMMENT ON THIS PAPER
 
 
 

 

 
 
 
 
 
 
 
 
 

 
 
 
 
 
 
 
 

       

       

Curve Bottom