Immobilized Biocatalysts of Eversa® Transform 2.0 and Lipase from Thermomyces Lanuginosus: Comparison of Some Properties and Performance in Biodiesel Production

Catalysts

Sara Arana-Peña¹  Malcom Yates¹  Cristina Otero¹  JavierA. Martínez-Sanchez¹  Diego Carballares¹  Roberto Fernandez-Lafuente¹ 

[1] ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain;

关键词: Eversa;    lipase from TLL;    interfacial activation;    enzyme stability;    enzyme specificity;    biodiesel;   

DOI  :  10.3390/catal10070738

来源: DOAJ

【 摘 要 】

Eversa^® Transform (ET), and the lipase from Thermomyces 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 °C and pH 7. Specific activity versus p-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 in tert-butanol medium, their performance was fairly similar.

【 授权许可】

Unknown