Performance of chloroperoxidase stabilization in mesoporous sol-gel glass using in situ glucose oxidase peroxide generation.
A unique mesoporous sol-gel glass possessing a highly ordered porous structure (with three pore sizes of about 50, 150, and 200 A 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., 200 A). 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.
Borole
Abhijeet
A
Oak Ridge National Laboratory, PO Box 2008, Oak Ridge, TN 37831-6226, USA. borolea@ornl.gov
Dai
Sheng
S
Cheng
Catherine L
CL
Rodriguez
Miguel
M
Davison
Brian H
BH
D000447:Aldehydes / Q000737:chemistry; D001709:Biotechnology / Q000379:methods*; D002384:Catalysis; D002711:Chloride Peroxidase / Q000737:chemistry*; D005949:Glucose Oxidase / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry; D006861:Hydrogen Peroxide / Q000737:chemistry; D008024:Ligands; D008956:Models, Chemical; D010545:Peroxides / Q000737:chemistry*; D044367:Phase Transition; D012821:Silanes / Q000737:chemistry; D012997:Solvents; D013696:Temperature
D000447:Aldehydes; D008024:Ligands; D010545:Peroxides; D012821:Silanes; D012997:Solvents; C005556:propionaldehyde; D006861:Hydrogen Peroxide; D005949:Glucose Oxidase; D006735:Horseradish Peroxidase; D002711:Chloride Peroxidase; C071717:trimethoxysilane