Cloning, heterologous expression and structural characterization of an alkaline serine protease from sea water haloalkaliphilic bacterium

2014 ◽  
Vol 65 (1) ◽  
pp. 371-381 ◽  
Author(s):  
Vikram H. Raval ◽  
Chirantan M. Rawal ◽  
Sandeep Pandey ◽  
Hitarth B. Bhatt ◽  
Bharat R. Dahima ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Serine Protease ◽  
Structural Characterization ◽  
Sea Water ◽  
Alkaline Serine Protease

Cloning, expression and characterization of a novel alkaline serine protease gene from native Iranian Bacillus sp.; a producer of protease for use in livestock

Gene ◽  
2019 ◽  
Vol 693 ◽  
pp. 10-15 ◽  
Author(s):  
Ahmadreza Ariyaei ◽  
Ayoub Farhadi ◽  
Fatemeh Moradian ◽  
Ghodrat Rahimi Mianji
Keyword(s):  
Serine Protease ◽  
Protease Gene ◽  
Bacillus Sp ◽  
Alkaline Serine Protease ◽  
Serine Protease Gene

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.

Heterologous expression and structural characterization of two low pH laccases from a biopulping white-rot fungus Physisporinus rivulosus

2012 ◽  
Vol 97 (4) ◽  
pp. 1589-1599 ◽  
Author(s):  
Kristiina Hildén ◽  
Miia R. Mäkelä ◽  
Taina Lundell ◽  
Jaana Kuuskeri ◽  
Alexey Chernykh ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Structural Characterization ◽  
Low Ph ◽  
White Rot ◽  
White Rot Fungus ◽  
Physisporinus Rivulosus

Characterization of an alkaline serine protease from an alkaline-resistant Pseudomonas sp.: Cloning and expression of the protease gene in Escherichia coli

1996 ◽  
Vol 18 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Won Hee Jang ◽  
Eun Kyung Kim ◽  
Hwanghee Blaise Lee ◽  
Jae Hoon Chung ◽  
Ook Joon Yoo
Keyword(s):  
Escherichia Coli ◽  
Serine Protease ◽  
Cloning And Expression ◽  
Protease Gene ◽  
Pseudomonas Sp ◽  
Alkaline Serine Protease

Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated Bacillus licheniformis NH1

2007 ◽  
Vol 40 (4) ◽  
pp. 515-523 ◽  
Author(s):  
Nedra El Hadj-Ali ◽  
Rym Agrebi ◽  
Basma Ghorbel-Frikha ◽  
Alya Sellami-Kamoun ◽  
Safia Kanoun ◽  
...  
Keyword(s):  
Serine Protease ◽  
Molecular Characterization ◽  
Bacillus Licheniformis ◽  
Alkaline Serine Protease
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