Dependency of Water Availability on the Esterifying Activity of Candida cylindracea Lipase in Organic Solvent

  • Moor, Izani (Fermentation and Enzyme Technology Laboratory, school of Biological sciences, Universiti Sains Malaysia) ;
  • Noor, Jamil (Fermentation and Enzyme Technology Laboratory, school of Biological sciences, Universiti Sains Malaysia) ;
  • Ibrahim che Omar (Fermentation and Enzyme Technology Laboratory, school of Biological sciences, Universiti Sains Malaysia)
  • Published : 2000.02.01

Abstract

To establish optimal conditions for esterification by Candida cylindracea, lipase reactions were performed simultaneously, separately, or individually in the varying initial rates of $0.014-0.060\mu$mole free fatty acids consumed min-1g-1. The reactants which were conditioned at aw of 0.12 gave the highest initial rate of esterifying $0.060\mu$mole free fatty acids consumed min-1g-1. These results suggest that the esterifying activity of lipase in an organic system depends on the transfer of available water within the reaction system.

Keywords

References

  1. Eur. J. Biochem. v.190 The control of lipase catalysed transesterification and esterification reaction rates: Effect of substrate polarity, water activity and the water molecules on enzyme activity. Goldberg, M.;D. Thomas;M. D. Legoy.
  2. Biotechnol. Bioeng. v.39 Organic solvents strip water off enzymes. Gorman, L. A.;J. S. Dordick.
  3. J. Res. Nat. Bur. Standards v.81A Humidity fixed point of binary saturated aqueous solutions. Greenspan, L.
  4. Enzyme Microb. Technol. v.16 Thermodynamic predictions for biocatalysis in non-conventional media: Theory, tests and recommendations for experimental design and analysis Halling, P. J.
  5. J. Biosci. v.6 Fixing water activity with saturated salt aqueous solution for biocatalysis in organic solvent. Ibrahim, C. O.;D. A. Robb.
  6. J. Mal. Appl. Biol. v.20 Esterification by lipase of Candida cylindracea with fatty acid distillates (FAD) as acyl donors. Ibrahim, C. O.;H. L. Tan
  7. Agric. Biol. Chem. v.51 no.3 Purification and some properties of a thermostable lipase from Humicola lanuginosa Ibrahim, C. O.;M. Hayashi;S. Nagai
  8. Tetrahedron v.48 Salt hydrates to buffer optimal water level during catalysed synthesis in organic media . A practical procedure for organic chemists Kvittinen, L. B.;Sjursnes;T. Anthosen;P. J. Halling
  9. Biotechnol. Bioeng. v.30 Rules for optimization of biocatalysis in organic solvent. Laane, C.;S. Boren;K. Vos;C. Voeger
  10. JAOCS v.53 Rapid colorimetric determination of free fatty acids Lowry, R. R.;I. J. Tinseley.
  11. Biopolymer v.33 The hydration of proteins in nearly anhydrous organic solvent suspensions. McMinn, J. H.;H. J. Sowa;S. B. Charnick;M. E. Paulitis
  12. Appl. Microb. Biotechnol. v.28 Lipase immobilization by adsorption: Effect of support hydrophobicity on the reaction rate of ester synthesis in cyclohexane Norin, M.;J. Boutelje;E. Holmberg;K. Hult
  13. Biochim. Biophys. Acta. v.1118 Reaction rate with lopase catalyst shows similar dependence of water activity in different organic solvents Valivety, R. H.;P. J. Halling;A. R. Macrae.
  14. Biotechnol. Bioeng. v.38 Solvents effect on biocatalysis in organic system: Equilibrium position and rates of lipase catalysed esterification Valivety, R. H.;G. A. Johnston;C. J. Suckling;P. J. Halling
  15. Enzyme Microb. Technol. v.14 Role of enzyme hydrophobicity in biocatalysis in biocatalysis in organic solvent. Vasques-Duhalt, R.;P. M. Fedorak;W. S. D. Westlake
  16. Biochim. Biophys. Acta v.1206 The solvent dependence of enzyme specificity. Wescott, C. R.;A. M. Klibanov.
  17. J. Biol. Chem. v.263 Enzymatic catalysis in non-aqueous solvents. Zaks, A.;A. M. Klibanov.