Neutral Serine Protease from Penicillium italicum. Purification, Biochemical Characterization, and Use for Antioxidative Peptide Preparation from Scorpaena notata Muscle

2014 ◽  
Vol 174 (1) ◽  
pp. 186-205 ◽  
Author(s):  
Ferid Abidi ◽  
Neyssene Aissaoui ◽  
Jean-Marc Chobert ◽  
Thomas Haertlé ◽  
Mohamed Nejib Marzouki
Keyword(s):  
Serine Protease ◽  
Biochemical Characterization ◽  
Penicillium Italicum ◽  
Antioxidative Peptide ◽  
Scorpaena Notata ◽  
Peptide Preparation

Extraction, purification, and biochemical characterization of serine protease from leaves of Abrus precatorius

2017 ◽  
Vol 47 (10) ◽  
pp. 1016-1024 ◽  
Author(s):  
Ngangoum Eric Serge ◽  
Mezajoug Kenfack Laurette Blandine ◽  
Sanjit Kumar ◽  
Tchiégang Clergé ◽  
Mookambeswaran Vijayalakshmi
Keyword(s):  
Serine Protease ◽  
Biochemical Characterization ◽  
Abrus Precatorius

scholarly journals Purification and Biochemical Characterization of Alkaline Serine Protease from Caesalpinia bonducella

2010 ◽  
Vol 5 (6) ◽  
pp. 1934578X1000500
Author(s):  
Hidayatullah Khan ◽  
Irshad Ali ◽  
Arif-ullah Khan ◽  
Mushtaq Ahmed ◽  
Zamarud Shah ◽  
...  
Keyword(s):  
Serine Protease ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Alkaline Serine Protease ◽  
Protease Enzyme ◽  
Caesalpinia Bonducella

A high molecular weight serine protease has been purified to electrophoretic homogeneity from the seeds of Caesalpinia bonducella Flem. (Caesalpiniaceae) by the combination of size exclusion and ion exchange chromatography. About 524 fold purification was achieved with an overall recovery of 6.8%. The specific activity was found to be 86 U/mg/min at pH 8.0. The calculated Km and Vmax were 1.66 mg/mL and 496.68 units/min per mg of protein, respectively. The molecular mass was estimated to be about 63 kDa by sodium dodecyl sulfate PAGE. The enzyme showed optimum activity at pH 8.0 and exhibited its highest activity at 40°C. The enzyme was strongly inhibited by 2mM phenylmethylsulfonyl fluoride (PMSF), suggesting the presence of a serine residue at the active site. PMSF showed a pure competitive type of inhibition with the serine protease enzyme. It was observed that enzyme activity was enhanced in the presence of dications and was active against a variety of modified substrates and natural proteins.

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