Lipases: Molecular structure and function

Abstract

Early reports on the production by both bacterial and eukaryotic cells of enzymes able to degrade lipid substrates date to over a century ago. Since then, research on lipolytic enzymes that includes lipases, esterases, phospholipases has been driven by their central roles in lipid metabolism and in signal transduction. Lipases are generally versatile enzymes that accept a broad range of substrates (i.e. aliphatic, alicyclic, bicyclic and aromatic esters, thioesters, activated amines) whilst maintaining high regio-, chemo- and enantioselectivity. The stability of most lipases in organic solvents paves the way for their exploitation in organic synthesis: in esterification, transesterification, aminolysis and oximolysis reactions (Drauz and Waldman, 1995). Such properties make lipases key players in the industrial enzyme sector (Schmid and Verger, 1998; Bornscheuer, 2000; Kirk et al., 2002; Jaeger and Eggert, 2002; Gupta et al., 2004). In this chapter we review the fundamental knowledge available on lipases, with particular emphasis on the relationship between the sequence, structure and function of those most commonly used in industrial processes. On the basis of this knowledge, novel and improved lipases may be generated, able to meet the requirements for robustness, selectivity and catalytic performances posed by modern biocatalysis. © 2007 Springer.