PURIFICATION AND PARTIAL CHARACTERIZATION OF AN ALKALINE LIPASE FROM PSEUDOMONAS PSEUDOALCALIGENES F-111

An extracellular alkaline lipase of alkalophilic Pseudomonas pseudoalc aligenes F-111 was purified to homogeneity. The apparent molecular wei ght determined by sodium dodecyl sulfate-polyacrylamide gel electropho resis was 32,000, and the isoelectric point was 7.3. With p-nitropheny l esters as its substrates, the enzyme shows preference for C-12 acyl and C-14 acyl groups. St was stable in the pH range of 6 to 10, which coincides crith the optimum pH range.