Lipolytic isoenzymes from Euphorbia latex

The activity and substrate specificity of latex lipases from Euphorbia species (E characias, E wulfenii pinea, E myrsinites and E. dendroides) were investigated. High lipolytic activity was found only in E. characias and for the first time in E wulfenii latex. For both species the lipolytic activity on various triglycerides, and under different temperature and pH conditions, in both crude latex and in partially purified enzymes was quantified. Optimised extraction and purification methods permitted the recovery of the enzymatic fraction with high lipolytic activity. This fraction is probably constituted by a pool of different lipolytic enzymes. Finally, lipolytic activity was also measured for E characias and E wulfenii during vegetative and reproductive stages. (C) 2003 Elsevier Ireland Ltd. All rights reserved.