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

Bioorg Med Chem. 2003 Mar 20;11(6):1041-6. doi: 10.1016/s0968-0896(02)00516-3.

Abstract

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.

MeSH terms

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

Substances

  • Bacterial Proteins
  • Enzyme Inhibitors
  • Esters
  • Fatty Acids
  • Solvents
  • Triglycerides
  • Carboxylic Ester Hydrolases
  • LipA protein, Pseudomonas
  • Lipase