Immobilization and Characterization of a Recombinant Thermostable Lipase (Pf2001)‎ from Pyrococcus furiosus on Supports with Different Degrees of Hydrophobicity

Abstract EN

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.