The major interest in the immobilization of enzymes is obtaining a biocatalyst with activity and stability that are not affected during the process when compared to the free enzyme. The application of lipases in industries requires the study of techniques suitable for reuse and stability increase such as immobilization strategies. This work studied the immobilization of lipases produced by solid state fermentation from Penicillium verrucosum using two hydrophobic supports: Accurel EP 1000 and activated carbon. For the lipase immobilization, 1 g of support was added to 50 mL of an enzyme solution and kept for 2 hour in an ice bath. The solution was then filtered and the immobilized enzyme was stored in a dissecator for 48 hour before the assays for lipase activity, protein, and specific lipase activity. The results showed that the lipase immobilized in activated carbon presented higher specific activity than the lipase immobilized in Accurel EP 1000. The use of activated carbon as support led to a specific activity of 1.5 × 10(6) U/mg of protein, yield of 30.42%, and retention of 382.516%.
Lipases; Penicillium verrucosum; immobilization
