Published: CABEQ 22 (1) (2008) 125–133
Paper type: Original Scientific Paper
D. S. Rodrigues, G. P. Cavalcante, A. L. O. Ferreira and L. R. B. Gonçalves
Abstract
The immobilization of Candida antarctica lipase type B on activated carbon was
studied. Adsorption conditions were investigated in order to improve enzyme activity
and stability in organic media. Results showed that biocatalyst activity and recovered activity were improved with increasing concentrations of ammonium sulphate on the
supernatant during enzyme adsorption. Hydrophobic interactions were the driving force
of the immobilization process. Nevertheless, the specific and recovered activity of the
immobilized enzyme is affected by pH of adsorption, and best results were obtained
when lipase adsorption was conducted near the enzyme isoeletric point (pI 6.0). Operational stability of the immobilized enzyme was markedly improved when lipase
loading was increased from 74.15 U g–1 to 112.34 U g–1. After the sixth cycle of butyl
butyrate synthesis, it retained around 10 % of the initial activity. Derivatives prepared in
this work were tested and compared to a commercial derivative and results showed that
they were a suitable biocatalyst to be used in the synthesis of flavours, such as butyl
butyrate.
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Keywords
Enzyme technology, activated carbon, lipase, immobilized enzyme, adsorption