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Purification and characterization of an alkaline lipase from a newly isolated Pseudomonas mendocina PK-12CS and chemoselective hydrolysis of fatty acid ester.

Bioorganic & Medicinal Chemistry

Bacterial Proteins, Carboxylic Ester Hydrolases, antagonists & inhibitors, chemistry, isolation & purification, Enzyme Inhibitors, pharmacology, Esters, Fatty Acids, Half-Life, Hydrogen-Ion Concentration, Hydrolysis, Lipase, Magnetic Resonance Spectroscopy, Mass Spectrometry, Pseudomonas, enzymology, Solvents, Spectrophotometry, Infrared, Substrate Specificity, Temperature, Triglycerides

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      Lipase isolated from a soil isolate, Pseudomonas mendocina (PK-12CS) chemoselectively hydrolyzed the fatty ester group in presence of arbamate of compound 5-amino-2,4-dihydro-3H-1,2,4-triazole-3 ones, a class of compounds which are attractive starting materials for the synthesis of triazole annealed heterocycles. The enzymatic method provides an easy access to the synthesis of N-substituted glycine. Under optimized fermentation conditions the culture produced 3510 Lipolytic Units/mL of cell free fermentation broth in 20 h of fermentation. The purified lipase exhibited molecular mass of 80 kDa on SDS polyacrylamide gel electrophoresis. The enzyme was stable at room temperature for more than a month and expressed maximum activity at 37 degrees C and pH 8.

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