Physicochemical properties of a lipase from pseudomonas fluorescens

  • Mamoru S
  • Tsutomu O
  • 1


    Mendeley users who have this article in their library.
  • 11


    Citations of this article.


The molecular weight of triacylglycerol lipase (EC from Pseudomonas fluorescens is estimated to be approx. 33 000 by sodium dodecyl sulfate electrophoresis and Sephadex G-75 gel filtration. The lipase appears to be a single-chain protein and contains neither sugar nor lipid. The enzyme has a sedimentation coefficient (s20,w) of 3.06, an intrinsic viscosity of 3.0 g/ml and a partial specific volume of 0.730 g/ml, with an isoelectric point of pH 4.46. Amino acid analysis showed that the enzyme contained few sulfur-containing amino acid residues with no disulfide links. The N-terminal residue of the enzyme was found to be alanine and optical rotation dispersion analysis showed that about 20% of the enzyme structure was in a helical configuration. © 1977.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Sugiura Mamoru

  • Oikawa Tsutomu

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free