ICP Instituto de Catalisis y Petroquímica

Diana F. Izquierdo, Oveimar Barbosa,,^b,c M. Isabel Burguete,^a Pedro Lozano,^d S.V. Luis,^a Roberto Fernadez-Lafuente^b* and Eduardo García-Verdugo^a*

^aDpt. Quimica Inorganica y Organica, Universidad Jaume I, Avda. Sos Baynat s/n, E-12071 Castellón, Spain.
^bDepartamento de Biocatálisis. Instituto de Catálisis y Petrolquímica-CSIC, Campus UAM-CSIC Madrid. Spain. 
^cEscuela de Química, Grupo de Investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia
^dUniversidad de Murcia, Facultad de Química, Departamento de Bioquímica y Biología Molecular B e Inmunología, Campus de Espinardo, E-30100 Murcia, Spain. 

Lipase B from Candida antarctica (CALB) is able to catalyze C-C bond formation.  After immobilization onto hydrophobic PS-DVB support, these activity increase when compared to that of the soluble or tan the commercially available Novozyme 435 (being up to 6 folds more active). Our results show that even although this activity is not related to the catalytic group, the promiscuous activities of CALB may be tuned via immobilization. In addition, we have show that the secondary structure of both immobilized enzymes is quite different, using FT-ATR-IR spectroscopy.