Kinetic study for the ethanolysis of fish oil catalyzed by lipozyme(®) 435 in different reaction media

J Oleo Sci. 2015;64(4):431-41. doi: 10.5650/jos.ess14263.

Abstract

The ethanolysis of fish oil in various reaction medium (tert-pentanol, n-hexane and solvent free system) catalyzed by the immobilized commercial lipase Lipozyme(®) 435 (Candida Antarctica) at atmospheric pressure has been studied in this work. The effect of some kinetic parameters, such as the amount of lipase, temperature and the initial reactant molar ratio ethanol:oil on monoacyglyceride and ethyl ester yield has been analyzed. Experimental data were successfully correlated by a simple kinetic model based on the elementary reactions proposed in this work. At high initial reactant molar ratio the three elementary steps can be considered as irreversible. However the reaction rate constants ratio for the deacylation of monoglyceride to glycerol decreased by decreasing the molar ratio ethanol:oil. The reaction rates are slower in n-hexane as reaction medium compared to tert-pentanol and a solvent-free system, at the experimental conditions essayed in this work. In this last case, ethanol acts as solvent for reaction and as reactant.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acylation
  • Animals
  • Atmospheric Pressure
  • Catalysis
  • Enzymes, Immobilized / chemistry
  • Esterification
  • Esters / chemistry
  • Ethanol / chemistry*
  • Fish Oils / chemistry*
  • Hexanes / chemistry
  • Kinetics
  • Lipase / chemistry*
  • Monoglycerides / chemistry
  • Pentanols / chemistry
  • Solvents
  • Temperature

Substances

  • Enzymes, Immobilized
  • Esters
  • Fish Oils
  • Hexanes
  • Monoglycerides
  • Pentanols
  • Solvents
  • n-hexane
  • Ethanol
  • Lipozyme
  • Lipase