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RevistaRSC Advances
Año2015
Volumen5
Páginas35801 - 35810
Internacional

VERSATILITY OF DIVINYLSUFONE SUPORTS PERMITS TO TUNING CALB PROPERTIES DURING ITS IMMOBILIZATION.

Autores:José Cleiton Sousa dos Santos, Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Jose C. S. dos Santosa,b,  Nazzoly Ruedaa,c, Alfredo Sanchezd,  Reynaldo
Villalongad, Luciana R.B. Gonçalvesb and Roberto Fernandez-Lafuentea*.
 
a: ICP-CSIC. Campus UAM-CSIC. Cantoblanco. 28049 Madrid. Spain.
b: Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
c Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.
d: Department of Analytical Chemistry, Faculty of Chemistry, Complutense University of Madrid, 28040 Madrid, Spain



The lipase B from C. antarctica (CALB) has been immobilized on divinylsulfone (DVS) activated agarose beads under different conditions (pH 5-10). In the presence of 0.3% of Triton X-100,  immobilization rate was rapid at pH 10 and the slowest one was that at pH 5. Incubation at pH 10 for 72 h of the immobilized enzymes before blocking of the support with ethylenediamine permitted to improve enzyme stability. Enzyme features (activity, stability, specificity versus different substrates, effect of the pH on enzyme properties) were quite different on the different CALB preparations, suggesting the different orientation of the enzyme. The alkaline incubation produced an increase in enzyme activity with some substrates, and some of the DVS-CALB preparations exhibited a higher specific activity than the octyl-preparations. The indirect fluorescence spectrum of the different immobilized preparations confirmed that different structures of the CALB molecules were generated after immobilization.
Palabras clave:Enzyme stabilization, Enzyme immobilization, interfacial activation, lipase properties tuning, lipase hyperactivation, divinylsulfone activated supports
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