Immobilization-Stabilization of Candida antarctica Lipase B in Agarose-Glyoxyl and Agarose-Octyl: Deactivation

• Main Authors: C. Belvera, J. J. Tamayoa, L. Molineroa, M. Laderoa, B. C. C. Pesselab, J. M. Guisánc, F. Garcia-ochoaa, Adpt Ingeniería Química, Facultad C. C
• Other Authors: The Pennsylvania State University CiteSeerX Archives
• Format: Text
• Language: English
• Subjects: Antarc*; Antarctica
• Online Access: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.581.1978; http://www.aidic.it/IBIC2008/webpapers/82Belver.pdf

Lipases are a well-known working-horse in the synthesis of several substances, mainly esters and amides. Their importance is increasing with time, with a high number of publications every year, in organic, analytical, and industrial chemistry, as well as in biochemistry and other health related sciences. CALB is the most used lipase in organic and industrial chemistry nowadays. On the other hand, glycerol is a good stabilizer for enzymes as well as a plentiful raw material whose market price is low due to the energy policy regarding biodiesel. This work is focused on the immobilization-stabilization of CAL-B for its use with glycerol, using both a mild and reversible immobilization, based on octyl-agarose, and an irreversible strong stabilizing immobilization on glyoxyl-agarose. The enzyme has been immobilized with and without a previous chemical modification based on the increase of amino groups on its surface. A kinetic study of the deactivation of the biocatalysts is presented to compare their performance in glycerol and other media, based on their activity and stability, being the octyl-agarose derivate the most promising for its use in glycerol. 1.