A study on the catalytic performance of lipase in reverse micelles

Chin J Biotechnol. 1991;7(4):301-7.

Abstract

The hydrolysis of olive oil catalyzed by Candida rugosa lipase solubilized in "H2O/AOT/isooctane" reverse micellar solution has been studied. The optimal conditions observed for lipase in reverse micelles were t = 25 degrees C, pH = 7.9, and R = [H2O]/[AOT] = 10. Lipase in reverse micelles is found to be quite stable. For example, after being incubated at 33 degrees C for 12 hours in AOT/isooctane with R = 5.4, the residual activity of lipase remains as high as 89%. No inhibition was observed even though the substrate concentration was increased up to 50% (v/v), and it was inhibited slightly when 40 mM Cu2+, Co2+ or Mn2+ ions were in the water pools.

MeSH terms

  • Candida / enzymology
  • Catalysis
  • Enzyme Activation
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Lipase / antagonists & inhibitors
  • Lipase / chemistry*
  • Lipase / drug effects
  • Metals / antagonists & inhibitors
  • Micelles*
  • Olive Oil
  • Plant Oils
  • Solvents
  • Temperature

Substances

  • Metals
  • Micelles
  • Olive Oil
  • Plant Oils
  • Solvents
  • Lipase