Immobilization and Characterization of a Recombinant Thermostable Lipase (Pf2001) from Pyrococcus furiosus on Supports with Different Degrees of Hydrophobicity.
We studied the immobilization of a recombinant thermostable lipase (Pf2001Δ60) from the hyperthermophilic archaeon Pyrococcus furiosus on supports with different degrees of hydrophobicity: butyl Sepabeads and octadecyl Sepabeads. The enzyme was strongly adsorbed in both supports. When it was adsorbed on these supports, the enzyme showed 140 and 237% hyperactivation, respectively. The assessment of storage stability showed that the octadecyl Sepabeads immobilized enzyme showed 100% of residual activity after 30 days of storage. However, the greatest stability at 70°C was obtained in butyl Sepabeads immobilized enzyme, which retained 77% activity after 1 hour incubation. The maximum activity of the immobilized preparations was obtained with the pH between 6 and 7, at 70°C. Thus, this study achieved a new extremophilic biocatalyst with greater stability, for use in several biotechnological processes.
Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, RJ 21941-909, Rio de Janeiro, Brazil.
Roberta Vieira
RV
Branco
Melissa Limoeiro
ML
Estrada Gutarra
Denise Maria Guimarães
DM
Freire
Rodrigo Volcan
RV
Almeida