scholarly journals Role of Intermolecular Disulfide Bonds of the Organic Solvent-Stable PST-01 Protease in Its Organic Solvent Stability

2001 ◽  
Vol 67 (2) ◽  
pp. 942-947 ◽  
Author(s):  
Hiroyasu Ogino ◽  
Takeshi Uchiho ◽  
Jyunko Yokoo ◽  
Reina Kobayashi ◽  
Rikiya Ichise ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Organic Solvents ◽  
Disulfide Bond ◽  
Disulfide Bonds ◽  
Site Directed Mutagenesis ◽  
Solvent Stability ◽  
Organic Solvent Tolerant ◽  
Intermolecular Disulfide Bonds ◽  
Solvent Tolerant ◽  
Solvent Stable

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.

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
Keyword(s):  
Organic Solvent ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant ◽  
Solvent Stable

Organic solvent stable protease isolation and characterization from organic solvent tolerant strain of Lysinibacillus sphaericus PAP02

Biologia ◽  
2016 ◽  
Vol 71 (9) ◽  
Author(s):  
Periasamy Anbu ◽  
Jae-Seong So ◽  
Byung-Ki Hur ◽  
Hyun-Shik Yun
Keyword(s):  
Organic Solvent ◽  
Lysinibacillus Sphaericus ◽  
Tolerant Strain ◽  
Isolation And Characterization ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant ◽  
Solvent Stable

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

A newly isolated organic solvent tolerant Bacillus sphaericus 205y producing organic solvent-stable lipase

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

A Newly Isolated Organic Solvent Tolerant Staphylococcus saprophyticus M36 Produced Organic Solvent-Stable Lipase

2006 ◽  
Vol 53 (6) ◽  
pp. 510-515 ◽  
Author(s):  
Yaowei Fang ◽  
Zhaoxin Lu ◽  
Fengxia Lv ◽  
Xiaomei Bie ◽  
Shu Liu ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Staphylococcus Saprophyticus ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant ◽  
Solvent Stable

scholarly journals New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

2019 ◽  
Vol 20 (6) ◽  
pp. 1264 ◽  
Author(s):  
Leelatulasi Salwoom ◽  
Raja Raja Abd. Rahman ◽  
Abu Salleh ◽  
Fairolniza Mohd. Shariff ◽  
Peter Convey ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Organic Solvents ◽  
Rice Bran Oil ◽  
Lipolytic Activity ◽  
Pseudomonas Sp ◽  
Lipase Gene ◽  
Cold Adapted ◽  
Organic Solvent Tolerant ◽  
Wide Range ◽  
Solvent Tolerant

In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarctic. Strain LSK25 lipase was successfully cloned, sequenced, and over-expressed in an Escherichia coli system. Sequence analysis revealed that the lipase gene of Pseudomonas sp. LSK25 consists of 1432 bp, lacks an N-terminal signal peptide and encodes a mature protein consisting of 476 amino acids. The recombinant LSK25 lipase was purified by single-step purification using Ni-Sepharose affinity chromatography and had a molecular mass of approximately 65 kDa. The final recovery and purification fold were 44% and 1.3, respectively. The LSK25 lipase was optimally active at 30 °C and at pH 6. Stable lipolytic activity was reported between temperatures of 5–30 °C and at pH 6–8. A significant enhancement of lipolytic activity was observed in the presence of Ca2+ ions, the organic lipids of rice bran oil and coconut oil, a synthetic C12 ester and a wide range of water immiscible organic solvents. Overall, lipase strain LSK25 is a potentially desirable candidate for biotechnological application, due to its stability at low temperatures, across a range of pH and in organic solvents.

Purification and characterization of organic solvent-stable lipase from organic solvent-tolerant Pseudomonas aeruginosa LST-03

2000 ◽  
Vol 89 (5) ◽  
pp. 451-457 ◽  
Author(s):  
Hiroyasu Ogino ◽  
Satoshi Nakagawa ◽  
Kaori Shinya ◽  
Toshiaki Muto ◽  
Nobuyuki Fujimura ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Organic Solvent ◽  
Purification And Characterization ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant ◽  
Solvent Stable
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