Purification and properties of a lipase from Cephaloleia presignis (Coleoptera, Chrysomelidae)

A novel lipase from the insect Cephaloleia presignis was purified by a proc edure involving ammonium sulphate precipitation, and Phenyl Toyopearl 650M, DEAE-5PW and hydrophobic-interaction column chromatographies. The purified lipase was homogeneous with a molecular mass of 31000 Da by SDS/PAGE and o f 29000 Da by gel filtration on a Superose IZ column. The enzyme was indent ified as a glycoprotein with a pi of 6.9. The enzyme unspecifically liberat ed short-chain to long-chain fatty acids from p-nitrophenyl esters, methyl esters and triglycerides. The hi-terminal 28 amino acid residues were deter mined as AGTLGYATRHVLPIFTLDDYTGSNEMWG, which showed no similarity with know n proteins, suggesting that the purified lipase may belong to a novel class of hydrolases.