Biocatalytic Performance of Chloroperoxidase from Caldariomyces fumago Immobilized onto TiO2 Based Supports
- 370 Downloads
Chloroperoxidase (CPO) from Caldariomyces fumago is a versatile enzyme able to catalyze the styrene epoxidation. However, the lack of long-term operational stability is the principal drawback for the industrial applications of this enzyme. In this work, in order to increase the enzyme operational stability, CPO immobilization in TiO2 mesoporous materials was studied. Enzyme immobilization onto two TiO2 supports was assayed: microstructured TiO2 anatase (TiO2AN) and nanostructured TiO2 nanotubes (TiO2NT). The CPO/TiO2NT preparation showed 15-times higher catalytic activity for styrene epoxidation than the free enzyme, showing an excellent performance during the styrene epoxidation. In addition, the total turnover numbers for styrene epoxidation, for the free and immobilized enzyme were determined. The CPO immobilization in TiO2 materials increased the operational stability of CPO in 51 % in the case TiO2AN and 69 % for TiO2NT support. These results clearly show that CPO immobilization onto TiO2NT support significantly enhances the CPO enzymatic epoxidation of styrene.
KeywordsEpoxidation Total turnover number Chloroperoxidase immobilization TiO2 nanotubes
F. A. Muñoz-Guerrero thanks to CONICYT for a graduate fellowship (Folio 63105502). Authors are grateful for the support of Conacyt-Conicyt International Cooperation Program (Folio PCCI130043) between México and Chile governments. REDOC CTA (Universidad de Concepción).
- 19.Hager LP, Morris DR, Brown FS, Eberwein H (1966) Chloroperoxidase: II. Utilization of halogen anions. J Biol Chem 241(8):1769–1777Google Scholar
- 20.Segel IH (1993) Enzyme kinetics: behavior and analysis of rapid equilibrium and steady-state enzyme systems. Wiley, New YorkGoogle Scholar
- 30.Thomas JA, Morris DR, Hager LP (1970) Chloroperoxidase: VII. Classical peroxidatic, catalityc, and halogenating forms of the enzyme. J Biol Inorg Chem 245(12):3129–3134Google Scholar