38
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      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

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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.

          Related collections

          Author and article information

          Comments

          Comment on this article