Hydrolases are enzymes which catalyze the hydrolytic cleavage of several organic
compounds, for example carboxylic acid esters and amides as well as their formation, and
the hydrolysis of nitriles and epoxides. Together they form the enzyme class 3 (EC 3), this
Enzyme Commission number is assigned by the International Union of Biochemistry and
Molecular Biology. Hydrolases are widely used in organic chemistry because they often
exhibit broad substrate specificity and do not require cofactors, which are costly and difficult
to regenerate, and due to the tolerance for organic solvents that many hydrolases (especially
lipases) exhibit. When water is removed from the reaction medium, it is often possible to shift
the equilibrium towards synthesis. Additionally, many hydrolases show a high
enantioselectivity which makes them attractive for the pharmaceutical industry and for the
synthesis of optically active building blocks for fine chemistry. While many esterases have
been described in literature, most technical applications use lipases which often exhibit a
broader substrate spectrum including water-insoluble substrates, better stability against
organic solvents and excellent enantioselectivities