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

作者: Veymar G. Tacias-Pascacio , Sara Peirce , Beatriz Torrestiana-Sanchez , Malcon Yates , Arnulfo Rosales-Quintero

DOI: 10.1039/C6RA21730C

关键词:

摘要: Five different commercial supports (Lifetech™ ECR1061M (styrene/methacrylic polymer), Lifetech™ ECR8804M (octadecyl methacrylate), ECR8806M methacylate), ECR1090M (styrene) and ECR1030M (DVB/methacrylic polymer)) were compared to octyl agarose in their performance the immobilization of four lipases (from Rhizomucor miehie (RML), from Thermomyces lanuginosus (TLL) forms A B Candida antarctica, (CALA CALB)) phospholipase Lecitase Ultra™ (LU). The new enzymatic derivatives evaluated with biocatalyst (Novozym 435 (CALB), Lipozyme RM IM TL IM). Textural properties, loading capacity, enzyme stability under conditions, activity versus substrates analyzed. Although all reversibly immobilized via interfacial activation hydrophobic surface support, some them permitted a significant improvement final reference support or preparations. Enzyme specificity depended strongly on used (e.g., ones gave almost null p-nitrophenyl butyrate). However, there is not universal optimal support; “best” depends enzyme, parameter studied substrate utilized. Nevertheless, conditions utilized, preparations showed very good diversity reactions reuse (both after eliminating by washing triton X-100). These will permit enlarging library lipase biocatalyst, being useful for aqueous organic medium.

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