[Isolation of the enzyme lipase from Pseudomonas fluorescens 533-5b and its characterization]

From the culture liquid of Pseudomonas fluorescens 533-5b, lipase (partially purified by sulphate ammonium precipitation and dialysis) was isolated. The following properties of the enzyme were examined: effect of pH and temperature, effect of bile salts, substrate specificity, and stability during storage. The optimal action of the preparation was at 55 degrees C and pH 7.5-8.0. Sodium salts of cholic, taurocholic, deoxycholic, and glycocholic acids at concentrations over 0.5%, as a rule, activated lipolysis. The enzyme preparation was stable during storage: activity losses were no more than 15% during a 2 month storage at 4 degrees C. Lipase of Ps. fluorescens 533-5b was capable to utilize as substrates many vegetable oils (olive, corn, castor, mustard) as well as synthetic triglycerides containing carboxylic acids with short and long carbon chains.