Abstract
Eversa(R)Transform (ET), and the lipase fromThermomyces lanuginosus(TLL), liquid commercial lipases formulations, have been immobilized on octyl agarose beads and their stabilities were compared. Immobilized and free ET forms were more thermostable than TLL formulations at pH 5.0, 7.0, and 9.0, and the ET immobilized form was more stable in the presence of 90% methanol or dioxane at 25 degrees C and pH 7. Specific activity versusp-nitrophenyl butyrate was higher for ET than for TLL. However, after immobilization the differences almost disappeared because TLL was very hyperactivated (2.5-fold) and ET increased the activity only by 1.6 times. The enzymes were also immobilized in octadecyl methacrylate beads. In both cases, the loading was around 20 mg/g. In this instance, activity was similar for immobilized TLL and ET using triacetin, while the activity of immobilized ET was lower using(S)-methyl mandelate. When the immobilized enzymes were used to produce biodiesel from sunflower oil and methanol intert-butanol medium, their performance was fairly similar.