scholarly journals Alkaline serine proteinase from Thermomonospora fusca YX. Stability to heat and denaturants

1991 ◽  
Vol 273 (3) ◽  
pp. 807-807
Keyword(s):  
Serine Proteinase ◽  
Thermomonospora Fusca ◽  
Alkaline Serine Proteinase

scholarly journals Alkaline serine proteinase from Thermomonospora fusca YX. Stability to heat and denaturants

1990 ◽  
Vol 270 (1) ◽  
pp. 51-55 ◽  
Author(s):  
M M Kristjansson ◽  
J E Kinsella
Keyword(s):  
Thermal Stability ◽  
Hydrophobic Interactions ◽  
Serine Proteinase ◽  
Sharp Decrease ◽  
Guanidinium Chloride ◽  
Thermomonospora Fusca ◽  
Ph Dependent ◽  
The Stability ◽  
Thermal Stability Of ◽  
Alkaline Serine Proteinase

The serine proteinase isolated from Thermomonospora fusca YX shows considerable thermal stability up to 80 degrees C, and progressive inactivation occurs at higher temperatures. Lyotropic salts affected the thermal stability of the enzyme at 85 degrees C, suggesting that disruption of hydrophobic interactions play an important role in the decreased thermal stability of the enzyme above 80 degrees C. Thermal stability is highly pH-dependent; above pH 6.0-6.5 there is a sharp decrease in the stability of the enzyme, reflecting increased autolysis. Although some stabilization occurs upon increasing ionic strength, Ca2+ binding does not appear to play a role in thermal stability. Denaturants, i.e. 8 M-urea, 6 M-guanidinium chloride or 1% SDS, had no significant effect on the activity of the enzyme after 24 h at 25 degrees C.

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.

Substrate specificity of alkaline serine proteinase isolated from photosynthetic bacterium, Rubrivivax gelatinosus KDDS1

2003 ◽  
Vol 309 (3) ◽  
pp. 547-551 ◽  
Author(s):  
Somporn Tanskul ◽  
Kohei Oda ◽  
Hiroshi Oyama ◽  
Napavarn Noparatnaraporn ◽  
Masahiko Tsunemi ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Serine Proteinase ◽  
Photosynthetic Bacterium ◽  
Rubrivivax Gelatinosus ◽  
Alkaline Serine Proteinase

scholarly journals Sequence of the Gene Encoding an Alkaline Serine Proteinase ofBacillus pumilusTYO-67

2000 ◽  
Vol 44 (5) ◽  
pp. 389-393 ◽  
Author(s):  
Misako Aoyama ◽  
Claudia Toma ◽  
Masaaki Yasuda ◽  
Masaaki Iwanaga
Keyword(s):  
Serine Proteinase ◽  
Gene Encoding ◽  
Alkaline Serine Proteinase

scholarly journals An Alkaline Serine-Proteinase from a Bacterium Isolated from Bat Feces: Purification and Characterization

2009 ◽  
Vol 73 (11) ◽  
pp. 2393-2398 ◽  
Author(s):  
Somporn TANSKUL ◽  
Kazumi HIRAGA ◽  
Katsumi TAKADA ◽  
Suchart RUNGRATCHOTE ◽  
Prasert SUNTINANALERT ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Purification And Characterization ◽  
Alkaline Serine Proteinase
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