Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion

Biotechnol Lett. 2008 Sep;30(9):1627-31. doi: 10.1007/s10529-008-9734-1. Epub 2008 Apr 22.

Abstract

Rhizomucor miehei lipase was immobilized in hydroxy(propylmethyl) cellulose or agar gels containing lecithin or AOT microemulsions. The effect of the diffusion of substrates and products to this catalyst was studied, as well as the effect of temperature on the initial rate of ester synthesis. The composition of the gel affects the reaction rate due to mass transport phenomena. The apparent activation energies were higher for the systems based on agar, independently of the microemulsion used, and lower for the systems based on AOT microemulsions, independently of the polymer used.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Propanol / metabolism
  • Catalysis
  • Diffusion
  • Emulsions
  • Enzyme Activation
  • Enzymes, Immobilized / metabolism*
  • Esterification
  • Gels
  • Heptanol / metabolism
  • Hypromellose Derivatives
  • Kinetics
  • Lauric Acids / metabolism
  • Lecithins / metabolism
  • Lipase / metabolism*
  • Methylcellulose / analogs & derivatives
  • Methylcellulose / metabolism
  • Rhizomucor / enzymology*
  • Substrate Specificity
  • Temperature*

Substances

  • Emulsions
  • Enzymes, Immobilized
  • Gels
  • Lauric Acids
  • Lecithins
  • lauric acid
  • Hypromellose Derivatives
  • Heptanol
  • Methylcellulose
  • 1-Propanol
  • Lipase