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Coimmobilization of pyranose 2-oxidase, laccase and catalase on solid supports for enhanced production of 2-keto aldoses

The tri-enzyme system pyranose 2-oxidase (P2O), laccase, and catalase was chosen to study the most influential parameters in the homogeneous and heterogeneous application of a complex redox machinery. P2O, which reduces oxygen or alternative electron acceptors and oxidizes aldoses to the corresponding 2-keto-sugars, was immobilized on eleven agarose or acrylic resins using varying coupling methods and the binding capacity was determined. An acrylic carrier (Amberzyme Oxirane) with the most suitable properties was selected for further testing. To increase the reaction rate, laccase was introduced to provide a competing electron acceptor, benzoquinone, which shows with P2O a three-fold higher turnover number than oxygen. Catalase was used to eliminate residual hydrogen peroxide and applied in different amounts to determine the influence of the hydrogen peroxide concentration on the turnover stability.

pyranose 2-oxidase; laccase; catalase; co-immobilization; 2-ketoglucose

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