Purification and Characterization of Alkaline Serine Proteinase from Photosynthetic Bacterium,Rubrivivax gelatinosusKDDS1

2004 ◽  
Vol 68 (3) ◽  
pp. 650-655 ◽  
Author(s):  
Kohei ODA ◽  
Somporn TANSKUL ◽  
Hiroshi OYAMA ◽  
Napavarn NOPARATNARAPORN
Keyword(s):  
Serine Proteinase ◽  
Photosynthetic Bacterium ◽  
Purification And Characterization ◽  
Alkaline Serine Proteinase

Purification and Characterization of Serine Proteinase from a Halophilic Bacterium,Filobacillussp. RF2-5

2005 ◽  
Vol 69 (1) ◽  
pp. 38-44 ◽  
Author(s):  
Kazumi HIRAGA ◽  
Yasushi NISHIKATA ◽  
Sirilak NAMWONG ◽  
Somboon TANASUPAWAT ◽  
Katsumi TAKADA ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Halophilic Bacterium ◽  
Purification And Characterization

scholarly journals Purification and characterization of a fibrinogenolytic serine proteinase fromAspergillus fumigatusculture filtrate

FEBS Letters ◽  
1992 ◽  
Vol 308 (1) ◽  
pp. 65-69 ◽  
Author(s):  
Gérald Larcher ◽  
Jean-Philippe Bouchara ◽  
Véronique Annaix ◽  
Françoise Symoens ◽  
Dominique Chabasse ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Purification And Characterization

scholarly journals Purification and characterization of the heat-stable serine proteinase from Thermomonospora fusca YX

1987 ◽  
Vol 246 (2) ◽  
pp. 511-517 ◽  
Author(s):  
T W Gusek ◽  
J E Kinsella
Keyword(s):  
Thermal Stability ◽  
Ionic Strength ◽  
Serine Proteinase ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Purification And Characterization ◽  
Thermomonospora Fusca ◽  
Heat Stable

The proteinase secreted from Thermomonospora fusca YX grown on cellulose was purified by (NH4)2SO4 fractionation and cation-exchange chromatography. The isolated proteinase readily hydrolysed several proteins and demonstrated activity towards casein from 35 to 95 degrees C (at pH 8.0) with maximum activity at 80 degrees C. It exhibited broad pH and ionic-strength optima centered at pH 9.0 and 0.2 M-NaCl respectively, and it retained high activity in the presence of 2% (w/v) SDS, 20 mM-dithiothreitol and 1.0 M-NaCl. The proteinase, which was fully inhibited by phenylmethanesulphonyl fluoride, had an Mr of 14,500 and an isoelectric point at 9.21. A measurement of proteinase thermal stability demonstrated a T50% (15 min) of 85 degrees C at pH 4.5.

Purification and characterization of a halotolerant serine proteinase from thermotolerant Bacillus licheniformis RKK-04 isolated from Thai fish sauce

2010 ◽  
Vol 86 (6) ◽  
pp. 1867-1875 ◽  
Author(s):  
Yoichi Toyokawa ◽  
Hiroaki Takahara ◽  
Alissara Reungsang ◽  
Masakazu Fukuta ◽  
Yuki Hachimine ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Serine Proteinase ◽  
Fish Sauce ◽  
Purification And Characterization
Sign in / Sign up

Export Citation Format

Share Document