A study on the catalytic performance of lipase in reverse micelles.
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.
Xu
J
J
Thermodynamics Research Laboratory, East China University of Chemical Technology, Shanghai.
Mao
Q
Q
Ying
X
X
Hu
Y
Y
D002175:Candida / Q000201:enzymology; D002384:Catalysis; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008049:Lipase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000187:drug effects; D008670:Metals / Q000037:antagonists & inhibitors; D008823:Micelles; D000069463:Olive Oil; D010938:Plant Oils; D012997:Solvents; D013696:Temperature
D008670:Metals; D008823:Micelles; D000069463:Olive Oil; D010938:Plant Oils; D012997:Solvents; D008049:Lipase