An Organic Solvent-tolerant Bacterium and Its Organic Solvent-stable Protease

1996 ◽  
Vol 799 (1 Enzyme Engine) ◽  
pp. 311-317 ◽  
Author(s):  
HIROYASU OGINO ◽  
KIYOSHI YASUI ◽  
FUMITAKE WATANABE ◽  
HARUO ISHIKAWA
Biologia ◽  
2016 ◽  
Vol 71 (9) ◽  
Author(s):  
Periasamy Anbu ◽  
Jae-Seong So ◽  
Byung-Ki Hur ◽  
Hyun-Shik Yun

AbstractIn this study, a bacterium producing solvent-stable protease was isolated from salt-enriched soil after incubation in benzene and toluene enriched-media and identified as


2003 ◽  
Vol 15 (2) ◽  
pp. 147-151 ◽  
Author(s):  
Chin John Hun ◽  
Raja Noor Zaliha Abd. Rahman ◽  
Abu Bakar Salleh ◽  
Mahiran Basri

2006 ◽  
Vol 53 (6) ◽  
pp. 510-515 ◽  
Author(s):  
Yaowei Fang ◽  
Zhaoxin Lu ◽  
Fengxia Lv ◽  
Xiaomei Bie ◽  
Shu Liu ◽  
...  

2001 ◽  
Vol 67 (2) ◽  
pp. 942-947 ◽  
Author(s):  
Hiroyasu Ogino ◽  
Takeshi Uchiho ◽  
Jyunko Yokoo ◽  
Reina Kobayashi ◽  
Rikiya Ichise ◽  
...  

ABSTRACT The PST-01 protease is secreted by the organic solvent-tolerant microorganism Pseudomonas aeruginosa PST-01 and is stable in the presence of various organic solvents. Therefore, the PST-01 strain and the PST-01 protease are very useful for fermentation and reactions in the presence of organic solvents, respectively. The organic solvent-stable PST-01 protease has two disulfide bonds (between Cys-30 and Cys-58 and between Cys-270 and Cys-297) in its molecule. Mutant PST-01 proteases in which one or both of the disulfide bonds were deleted were constructed by site-directed mutagenesis, and the effect of the disulfide bonds on the activity and the various stabilities was investigated. The disulfide bond between Cys-270 and Cys-297 in the PST-01 protease was found to be essential for its activity. The disulfide bond between Cys-30 and Cys-58 played an important role in the organic solvent stability of the PST-01 protease.


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