Purification and characterization of a Penicillium sp. lipase which discriminates against diglycerides

Lipids. 1996 Apr;31(4):379-84. doi: 10.1007/BF02522923.

Abstract

A lipase was isolated from Penicillium sp. strain UZLM-4 and characterized. This lipase has a molecular weight of 27,344 (determined by mass spectrometry) and hydrolyzes triglycerides in preference to mono- and diglyceride substrates. Among various triglyceride substrates, tributyrin is hydrolyzed about four times faster than any other tested. The lipase has a preference for hydrolysis at the 1,3 positions of the lipids and shows a weak stereoselectivity for the S enantiomer. Unlike most other lipases, this lipase is stable and has a high activity at low surface pressures (5-10 mN/m).

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Diglycerides / metabolism*
  • Glycerides / metabolism
  • Kinetics
  • Lipase / chemistry
  • Lipase / isolation & purification*
  • Lipase / metabolism*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Molecular Weight
  • Penicillium / enzymology*
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Pressure
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Surface Properties
  • Triglycerides / metabolism

Substances

  • Diglycerides
  • Glycerides
  • Peptide Fragments
  • Triglycerides
  • Lipase
  • tributyrin