Bioprocess and Biosystems Engineering

, Volume 31, Issue 4, pp 323–327 | Cite as

Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis

  • L. Costa
  • V. Brissos
  • F. Lemos
  • F. Ramôa Ribeiro
  • J. M. S. Cabral
Original Paper


The activity of various lipases was compared, in both free and immobilized forms, using the kinetics of the hydrolysis reaction of p-nitrophenyl butyrate, which was followed with in situ UV/Vis diode array spectrophotometry. Several enzymes were used to catalyze the reaction, namely Candida antarctica lipase B and Fusarium solani pisi cutinase wildtype and three single-mutation variants. The enzymes were tested in three different forms: free, immobilized as cross-linked aggregates and supported on zeolite NaY. A simple kinetic model was used to allow a quantitative comparison of the behavior of the different catalysts. It was concluded that although immobilization reduces the activity of the enzyme, the zeolite offers a much higher specific activity when compared to the cross-linked aggregates, thus supplying a heterogeneous catalyst with promising catalytic properties.


Lipases Zeolite NaY Kinetic modeling Diode array spectrophotometry Spectral deconvolution 



The authors gratefully thank Novozymes A/S (Denmark) for the kind gifts of Novozym® 435 and Lipozyme® CALB L. L. Costa and V. Brissos acknowledge Ph.D. grants (SFRH/BD/19108/2004 and SFRH/BD/9019/2002) from Fundação para a Ciência e Tecnologia.


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Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • L. Costa
    • 1
  • V. Brissos
    • 1
  • F. Lemos
    • 1
  • F. Ramôa Ribeiro
    • 1
  • J. M. S. Cabral
    • 1
  1. 1.IBB—Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical EngineeringInstituto Superior TécnicoLisboaPortugal

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