Flavobacterium odoratum lipase: Isolation and characterization

An extracellular lipase from Flavobacterium odoratum was purified 14-fold with 18% recovery by three-phase partitioning, anion-exchange chromatography, and hydroxylapatite chromatography. The purified enzyme had a monomeric molecular mass of approximately 32,500. The enzyme is fairly thermostable and has an optimum temperature between 50–65°C. An alkali optimum pH was observed between pH 9.0–10.5. A wide substrate specificity with a preference toward esters of unsaturated fatty acids was obtained. The effect of metal ions indicated that the enzyme was probably metal ion dependent.