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PublicationEnzyme and Microbial Technology
Year2017
Volume96
Pages 30-35
International

Relevance of substrates and products on the desorption of lipases physically adsorbed on hydrophobic supports

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Jose J. Virgen-Ortíz 1,2, +, Veymar G. Tacias-Pascacio 1,3,+, Daniela B. Hirata 4,
Beatriz Torrestiana-Sanchez 3, Arnulfo Rosales-Quintero 5, Roberto Fernandez-Lafuente 1*


Lipase B from Candida antarctica (CALB) has been physically immobilized on octyl-agarose via interfacial activation. The incubation of the enzyme in 80% ethanol at pH 5 and 25 ºC has not significant effect on enzyme activity. Moreover, the hydrolysis of 100 mM tributyrin catalyzed by this biocatalyst exhibited a quite linear reaction course. However, a new cycle of tributyrin hydrolysis showed a drastic drop in the activity. SDS-PAGE gels of the supernatant and the biocatalyst showed a significant enzyme desorption after the reaction. Similar results could be appreciated using triacetin or sunflower oil, while using 300 mM methyl phenyl acetate, butyl butyrate or ethyl butyrate most enzyme molecules remained immobilized. The results show that the detergent properties of some reaction products increase the enzyme release from the hydrophobic support, and this problem increased if the concentration of the reactants increased. Using 500 mM tributyrin, even in fully aqueous medium, some enzyme desorption from the support may be observed. Thus, the results show a limitation of this kind of biocatalysts that should be considered in the selection of an industrial lipase biocatalyst. 
Keywords:lipase interfacial activation/ octyl agarose/ detergents/ enzyme leakage/ enzyme reuse. 
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