| Summary: | Trabajo presentado en el 16th European Congress on Biotechnology, celebrado en Edimburgo (Escocia) del 13 al 16 de julio de 2014. Chemical modification of enzymes can be used to modulate enzyme properties by means of modification of protein surface or key residues from the enzyme structure [1,2]. In this work, it was carried out chemical modifications of Candida antarctica lipase B (CALB) preparations immobilized on octyl-agarose, BrCN-agarose and Eupergit-C supports using different chemical compounds, e.g. ethylenediamine (EDA), succinic anhydride (SA) and 2,4,6- trinitrobenzensulfonic acid (TNBS). These modifications of the enzyme surface caused changes in physical properties such as charge (isoelectric point) or hydrophobicity (solubility), and proved to be practical methods to enhance the biocatalyst performance (stability, activity and enantio-selectivity) when the enzyme preparations were submitted to different ranges of pH (4-9) and temperature (25-70 ¿C) and organic co-solvents such as acetonitrile or tetrahydrofuran at 50% (v/v). These immobilized and chemically modified CALB preparations displayed high enantioselectivity during the kinetic resolution of (R/S)-methyl mandelate in aqueous solution and esterification of beta-blocker drugs such as atenolol and propranolol. These alterations in enzyme properties by chemical modification should be due to changes in the structure of the active form of CALB. Therefore, solid phase chemical modification of immobilized lipases may become a powerful tool in the design of lipase libraries with very different properties. Peer Reviewed
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