Performance of Chloroperoxidase Stabilization in Mesoporous Sol-Gel Glass Using In Situ Glucose Oxidase Peroxide Generation

2004; Humana Press; Linguagem: Inglês

10.1007/978-1-59259-837-3_23

Autores

Abhijeet P. Borole, Sheng Dai, Catherine L. Cheng, Miguel Rodríguez, Brian H. Davison,

Tópico(s)

Mesoporous Materials and Catalysis

Resumo

A unique mesoporous sol-gel glass possessing a highly ordered porous structure (with three pore sizes of about 50, 150, and 200Å diameter) was used as a support material for immobilization of the enzyme chloroperoxidase (CPO). CPO was bound onto the glass via a bifunctional ligand, trimethoxysilylpropanal. In situ production of the cosubstrate, H2O2 was achieved using glucose oxidase. Solvent stability in acetonitrile mixtures was enhanced when a pore size larger than the size of CPO was used (i.e., 200Å). From these results, it appears that the glass-enzyme complex developed through the present work can be used as high-performance biocatalysts for various chemical-processing applications, particularly in harsh conditions.

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