Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia

  • Flóra Nagy Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, Hungary
  • Kinga Szabó Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, Hungary
  • Péter Bugovics Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, Hungary
  • Gábor Hornyánszky Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology Budapest University of Technology and Economics, Műegyetem rkp. 3, H-1111 Budapest, Hungary; SynBiocat LLC., Szilasliget u. 3, H-1172 Budapest, Hungary

Abstract

An efficient and easy-to-perform method was developed for covalent immobilization of lipase from Burkholderia cepacia (Lipase PS) on hollow silica microspheres (M540) by bisepoxide activation. For immobilization, various bisepoxides of different length, rigidity and hydrophobicity in their linkers were applied to activate the amino groups on the M540 support. Effect of the individual bisepoxides on the catalytic performance of the immobilized Lipase PS was studied by using lipase-catalyzed kinetic resolution (KR) of racemic 1-phenylethanol (rac-1) with vinyl acetate in batch mode. Catalytic activity, enantiomer selectivity, recyclability and thermal stability of the new immobilized Lipase PS biocatalysts were investigated. The optimal enzyme / support ratio with the support activated by the most efficient bisepoxide, i.e. poly(ethylene glycol) diglycidyl ether (PDE), was 1:5. The most efficient Lipase PS on PDE activated M540 showed an almost five fold higher biocatalytic activity value (rbatch = 42.8 U/g) with enhanced selectivity (ee(R)-2 = 99.1 %) to the free form of Lipase PS (rbatch = 9.0 U/g; ee(R)-2 = 98.9 %). The Lipase PS on PDE-M540 was compared to a commercially available immobilized Lipase PS biocatalyst (Lipobond Lipase PS) and also applied in a packed-bed enzyme reactor operated in continuous-flow mode, where the optimal temperature of M540-PDE-PS reached the 70 °C, while the optimum for Lipobond Lipase PS was 50 °C.

Keywords: Lipase PS, surface modification, covalent immobilization, kinetic resolution, continuous-flow reactor
Published online
2019-02-28
How to Cite
Nagy, F., Szabó, K., Bugovics, P. and Hornyánszky, G. (2019) “Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia”, Periodica Polytechnica Chemical Engineering, 63(3), pp. 414-424. doi: https://doi.org/10.3311/PPch.12665.
Section
Articles