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PublicationRSC Advances
Pages 100281 - 100294

Evaluation of different commercial hydrophobic supports for the immobilization of lipases: tuning their stability, activity and specificity.

Authors:Roberto Fernandez-Lafuente, Malcolm Yates Buxcey
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos, Usos avanzados de Ecomateriales procedentes de la industria agroalimentaria
Veymar G. Tacias-Pascacio,ab  Sara Peirce,ac Beatriz Torrestiana-Sanchez,b  Malcon Yates,a Arnulfo Rosales-Quintero,d Jose J. Virgen-Ortíz,*a,e and Roberto Fernandez-Lafuente*a

Five different commercial supports (Lifetech™ ECR1061M (Styrene/methacrylic polymer), Lifetech™ ECR8804M (Octadecyl methacrylate), Lifetech™ ECR8806M (Octadecyl methacylate), Lifetech™ ECR1090M (Styrene) and Lifetech™ ECR1030M (DVB/methacrylic polymer)) were compared to octyl agarose in their performance in the immobilization of four different lipases (from  Rhizomucor  miehie  (RML), from  Thermomyces lanuginosus (TLL) and the forms A and B from Candida antarctica, (CALA and CALB)) and of the phospholecitase Lecitase Ultra (LU). The characteristics of the new enzymatic derivatives were evaluated and compared with the properties of commercial biocatalyst (Novozym 435 (CALB), Lipozyme RM IM and Lipozyme TL IM). Textural properties, loading capacity, enzyme stability under different conditions, and activity versus different substrates were analyzed.  It was shown that among the new supports, some permitted a significant improvement in the final biocatalyst compared to the reference or the commercial preparations. Enzyme specificity depended strongly on the used support (e.g., the new ones gave almost null activity versus p-nitrophenyl butyrate). However, there is not a universal optimal support; the “best” support depends on the enzyme, the parameter studied and the substrate utilized. Nevertheless, under the conditions utilized, the preparations showed a very good performance in a diversity of reactions and permitted their reuse (both the biocatalyst and the supports). These supports will permit enlarging the library of immobilized lipase biocatalyst, being supports useful for aqueous or organic medium.  

Keywords:Hydrophobic supports, Lipase immobilization, reversible immobilization, Interfacial activation of lipase, tuning of lipase properties by immobilization
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