Biotechnology and Bioprocess Engineering

, Volume 18, Issue 6, pp 1090–1100 | Cite as

Catalytic properties of lipases immobilized onto ultrasound-treated chitosan supports

  • Matheus Dorneles de Mello
  • Deborah Cordeiro
  • Lilian Terezinha Costa
  • Cristian Follmer
Research Paper


Ultrasound sonication has been utilized to produce fragmentation of chitosan polymer and hence increase the chitosan surface area, making it more accessible to interactions with proteins. In this context, we have investigated the catalytic properties of lipases from different sources immobilized onto ultrasound-treated chitosan (ChiS) pre-activated with glutaraldehyde (ChiS-G). Atomic force microscopy indicated that ChiS-G displays a more cohesive frame without the presence of sheared/fragmented structures when compared with ChiS, which might be attributed to the cross-linking of the polysaccharide chains. The immobilization efficiency onto ChiS-G and ChiS were remarkably higher than using conventional beads. In comparison with the free enzymes, lipases immobilized onto ChiS show a slight increase of apparent Km and decrease of apparent Vmax. On the other hand, immobilization onto ChiS-G resulted in an increase of Vmax, even though a slight increase of Km was also observed. These data suggest that the activation of chitosan with glutaraldehyde has beneficial effects on the activity of the immobilized lipases. In addition, the immobilization of the lipases onto ChiS-G displayed the best reusability results: enzymes retained more than 50% of its initial activity after four reuses, which might be attributed to the covalent attachment of enzyme to activated chitosan. Overall, our findings demonstrate that the immobilization of lipases onto ultrasound-treated chitosan supports is an effective and low-cost procedure for the generation of active immobilized lipase systems, being an interesting alternative to conventional chitosan beads.


lipases chitosan ultrasound cross-linking glutaraldehyde 


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Copyright information

© The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Matheus Dorneles de Mello
    • 1
  • Deborah Cordeiro
    • 1
  • Lilian Terezinha Costa
    • 2
    • 3
  • Cristian Follmer
    • 1
  1. 1.Department of Physical Chemistry, Institute of ChemistryFederal University of Rio de JaneiroRio de JaneiroBrazil
  2. 2.National Institute of MetrologyStandardization and Industrial QualityDuque de CaxiasBrazil
  3. 3.Institute of BiophysicsFederal University of Rio de Janeiro/XerémDuque de CaxiasBrazil

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