The recent progress in knowledge on biochemical properties and functions of phospholipases A(2) in plants paved the way for approving the suitability of these enzymes for commercial use now. The secreted phospholipases A(2), representing one type of phospholipases A(2) occurring in plants, show distinct differences in substrate specificities with respect to headgroup and acyl chains of the glycerophospholipids in comparison to their counterparts from animal sources. The other type of phospholipases A(2) in plants, the patatin-related phospholipases A(2), is characterized by broad substrate specificity. Accordingly, the unique properties of the plant enzymes open new horizons to engineered biocatalysts with improved performance, e.g., for vegetable oil refinement by degumming and for targeted modification of phospholipids.