Abstract: A lipase variant of a parent lipase comprising a trypsin-like catalytic triad including an active serine located in a predominantly hydrophobic, elongated binding pocket of the lipase molecule and, located in a critical position of a lipid contact zone of the lipase structure, an amino acid residue different from an aromatic amino acid residue, which amino acid residue interacts with a lipid substrate at or during hydrolysis, in which lipase variant said amino acid residue has been replaced by an aromatic amino acid residue so as to confer to the variant an increased specific activity as compared to that of the parent lipase. The parent lipase may be a C. antarctica lipase A essentially free from other substances from C. antarctica, which comprises the amino acid sequence shown in SEQ ID No. 2, or a variant of said lipase which (1) has lipase activity, (2) reacts with an antibody reactive with at least one epitope of C. antarctica lipase A having th eamino acid sequence SEQ ID No.