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Physical crosslinking of lipase from Rhizomucor miehei immobilized on octyl agarose via coating with ionic polymers. Avoiding enzyme release from the support

Autores:Roberto Fernandez-Lafuente, Cristina Otero Hernández
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos, Biocatalisis y Bioenergía (GBB)
Laura Fernandez-Lopez, Sara G. Pedrero, Nerea Lopez-Carrobles, Jose J. Virgen-Ortíz, Beatriz C. Gorines, Cristina Otero, Roberto Fernandez-Lafuente*

Lipase from Rhizomucor miehei (RML) was immobilized on octyl-agarose (OC) at different loadings. Using low enzyme loadings (1/7 of the maximum loading), the incubation of the enzyme with polyethylenimine (PEI) increased the resistance to enzyme desorption in the presence of Triton X-100. However, more than 10% of the enzyme activity could be released from the OC-RML-PEI. The same treatment using fully loaded biocatalyst reduced the enzyme desorption to less than 5%. Further treatment with dextran sulfate (DS) of the PEI treaded immobilized enzyme fully avoids the enzyme desorption even in presence of a Triton X-100 concentration higher than that required for the complete enzyme release  from OC-RML. This treatment produced a high stabilization of OC-RML in thermal or organic solvent inactivations, reducing the enzyme release under these drastic conditions. Nevertheless, the support could be recovered by incubation under adequate conditions, and reused in several adsorption/desorption cycles. Thus, the strategy permitted to avoid enzyme desorption, very likely by physical intermolecular crosslinking improving enzyme stability, while still maintaining the reversibility of the immobilization

Palabras clave:Enzyme stabilization, Hydrophobic supports, Lipase immobilization, interfacial activation, enzyme desorption, support reuse
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