Dibenzothiophene biodegradation by a Pseudomonas sp. in poorly degradable organic solvents

1996 ◽  
Vol 31 (7) ◽  
pp. 711-717 ◽  
Author(s):  
Walter Maria Julia De Fatima ◽  
Leonardo Setti ◽  
Gaetano Lanzarini ◽  
Pier Giorgio Pifferi
1998 ◽  
Vol 64 (5) ◽  
pp. 1929-1932 ◽  
Author(s):  
Noriyuki Doukyu ◽  
Rikizo Aono

ABSTRACT Extracellular cholesterol oxidase of Pseudomonas sp. strain ST-200 was purified from the culture supernatant. This oxidase contained bound flavin and was categorized as a 3β-hydroxysteroid oxidase, converting 3β-hydroxyl groups to keto groups. The molecular mass was 60 kDa. The enzyme was stable at pH 4 to 11 and active at pH 5.0 to 8.5, showing optimal activity at pH 7 at 60�C. The Michaelis constant of the ST-200 cholesterol oxidase was lower than those of commercially available oxidases. The cholesterol oxidation rate was enhanced 3- to 3.5-fold in the presence of organic solvents, with log P ow values (partition coefficients of the organic solvent betweenn-octanol and water), in the range of 2.1 to 4.2, compared with that in the absence of organic solvents.


2019 ◽  
Vol 20 (6) ◽  
pp. 1264 ◽  
Author(s):  
Leelatulasi Salwoom ◽  
Raja Raja Abd. Rahman ◽  
Abu Salleh ◽  
Fairolniza Mohd. Shariff ◽  
Peter Convey ◽  
...  

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.


2008 ◽  
Vol 48 (6) ◽  
pp. 473-479 ◽  
Author(s):  
Hye Jung Choi ◽  
Seon-A Kim ◽  
Dong Wan Kim ◽  
Ja Young Moon ◽  
Yong Kee Jeong ◽  
...  

ChemInform ◽  
2010 ◽  
Vol 23 (31) ◽  
pp. no-no ◽  
Author(s):  
H. HIRATA ◽  
K. SAKAKI ◽  
T. YAMASHINA ◽  
K. HIGUCHI ◽  
H. YANAGISHITA ◽  
...  

1960 ◽  
Vol XXXV (I) ◽  
pp. 34-48 ◽  
Author(s):  
Gerd Ittrich

ABSTRACT A series of organic solvents and phenol derivatives have been examined for the extraction of the pink Kober-colour complex. Optimal results could be achieved for fluorimetry by a solution of 2 % (w/v) p-nitrophenol and 1 % (v/v) ethanol in acetylenetetrabromide, when the green mercury line (546 mμ was used as primary light. The sensitivity, stability and specificity have been improved, compared with the previously described reaction. By changing the sequence of purification steps and by reducing the volume of the urine sample (5 ml) the method for the determination of total oestrogens has been simplified. Approximately 10 determinations can be done within 3–4 hours by one person. Recovery experiments and comparative determinations with a previously described method have been carried out. The excretion of total oestrogens in a complete menstrual cycle is determined with the described method.


2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  

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