Abstract
Several research groups reported that lipase catalyzes peptide synthesis in organic solvents. Structural studies revealed that the catalytic triad of lipase consists of Ser, His, and Asp, the same as serine proteases. Lipase has a potential to have peptidase activity. In this report, we investigated the peptidase activity of lipases. Of 13 lipases of diverse origin tested, only commercially available porcine pancreatic lipase (PPL) exhibited peptidase activity. However, purification of PPL by gel permeation chromatography separated the peptidase and lipolytic activities of PPL. This study clearly demonstrated that all the lipases tested do not hydrolyze a peptide bond.
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