Evidence of surfactin hydrolysis by a bacterial endoprotease

The V8 endoprotease from Staphylococcus aureus hydrolyzes the cyclic lipope ptide, surfactin, at 100 mu M. The fragmentation lies between the two resid ues L-Glu1 and L-Leu2 leading to an open-chain lipopeptide. The structure o f the product arising from the enzymic hydrolysis was established by chemic al methods and mass spectrometry. The enzyme action has been suggested to b e likely limited by the aggregation state of the lipopeptide in solution.