Recent advances in the purification, characterization and structure determination of lipases

Abstract

Recently, lipases have been purified from mammalian, bacterial, fungal and plant sources by different methodologies. Purified lipases subsequently have been characterized for molecular size, metal binding capabilities, glycoside and phosphorus contents, and substrate specificities. Primary structures of several lipases have been determined either from amino acid or nucleic acid sequences. Lipases sequenced to date share sequence homologies including a significant region, Gly-X-Ser-X-Gly, that is conserved in all. The Ser residue is suspected to be essential for binding to lipid substrates.