ChemInform Abstract: Solvent Effect on Pseudomonas sp. Lipase Catalyzed Transesterification Between Tributyrin and 2-Octanol in Organic Solvents.

ChemInform ◽  
2010 ◽  
Vol 23 (31) ◽  
pp. no-no ◽  
Author(s):  
H. HIRATA ◽  
K. SAKAKI ◽  
T. YAMASHINA ◽  
K. HIGUCHI ◽  
H. YANAGISHITA ◽  
...  
1973 ◽  
Vol 19 (12) ◽  
pp. 1523-1526 ◽  
Author(s):  
D. W. Stranks

Phenethyl alcohol and some other specific solvents enhanced the production of cellulase by several fungi when added to culture growth media in minimal amounts. This solvent effect is considered to be cytoplasmic membrane-oriented. Cellulase synthesis possibly occurs in the same region of the cell.


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.


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