Guanidine hydrochloride-induced denaturation of Pseudomonas cepacia lipase

J Biochem. 1999 Aug;126(2):382-6. doi: 10.1093/oxfordjournals.jbchem.a022461.

Abstract

The guanidine hydrochloride-induced denaturation of Pseudomonas cepacia lipase (PCL) was studied at pH 7 by monitoring the changes in the fluorescence and circular dichroism of the enzyme. The denaturation was irreversible as a whole, and the addition of Ca2+ ions decreased the velocity of the denaturation. The denaturation process was well explained consistently by a two-step mechanism, as follows: [see equation in text] where N is the native state of PCL, D(I) an intermediate denatured-state which can be refolded into the native state, and D(F) the final denatured-state that can not be renatured. Ethanol (10%) increased the denaturation velocity by decreasing the refolding step, D(I) + Ca2+ --> N x Ca2+, which would be caused by the stabilization of D(I) by ethanol.

MeSH terms

  • Burkholderia cepacia / enzymology*
  • Calcium / metabolism
  • Circular Dichroism
  • Dose-Response Relationship, Drug
  • Ethanol / pharmacology
  • Guanidine / pharmacology*
  • Hydrogen-Ion Concentration
  • Ions
  • Kinetics
  • Lipase / chemistry*
  • Lipase / drug effects*
  • Protein Denaturation
  • Spectrometry, Fluorescence
  • Temperature
  • Thermodynamics
  • Time Factors

Substances

  • Ions
  • Ethanol
  • Lipase
  • Guanidine
  • Calcium