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Purification and properties of a lipase from Cephaloleia presignis (Coleoptera, Chrysomelidae)
Author(s) -
ArreguínEspinosa Roberto,
Arreguín Barbarín,
González Carolina
Publication year - 2000
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba19990088
Subject(s) - lipase , triacylglycerol lipase , size exclusion chromatography , chromatography , molecular mass , enzyme , chemistry , ammonium , biochemistry , amino acid , organic chemistry
A novel lipase from the insect Cephaloleia presignis was purified by a procedure 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 of 29000 Da by gel filtration on a Superose 12 column. The enzyme was indentified as a glycoprotein with a pI of 6.9. The enzyme unspecifically liberated short‐chain to long‐chain fatty acids from p ‐nitrophenyl esters, methyl esters and triglycerides. The N‐terminal 28 amino acid residues were determined as AGTLGYATRHVLPIFTLDDYTGSNEMWG, which showed no similarity with known proteins, suggesting that the purified lipase may belong to a novel class of hydrolases.