Coimmobilization of a redox enzyme and a cofactor regeneration system.
The coimmobilization of nitrobenzene nitroreductase and glucose-6-phosphate dehydrogenase in silica particles enables the continuous conversion of nitrobenzene to hydroxylaminobenzene with NADPH recycling.
Betancor
Lorena
L
Air Force Research Laboratory, 139 Barnes Drive, Suite #2, Tyndall AFB, FL 32403-5323, USA.
Berne
Cécile
C
Luckarift
Heather R
HR
Spain
Jim C
JC
D004800:Enzymes, Immobilized / Q000737:chemistry*; D005954:Glucosephosphate Dehydrogenase / Q000737:chemistry*; D006898:Hydroxylamines / Q000138:chemical synthesis / Q000737:chemistry; D015394:Molecular Structure; D009249:NADP / Q000737:chemistry*; D009578:Nitrobenzenes / Q000737:chemistry; D009601:Nitroreductases / Q000737:chemistry*; D010084:Oxidation-Reduction; D010316:Particle Size; D012822:Silicon Dioxide / Q000737:chemistry; D013499:Surface Properties; D013997:Time Factors
D004800:Enzymes, Immobilized; D006898:Hydroxylamines; D009578:Nitrobenzenes; C012484:phenylhydroxylamine; D009249:NADP; D012822:Silicon Dioxide; C036077:nitrobenzene; C029492:aromatic NADH-dependent nitroreductase; D005954:Glucosephosphate Dehydrogenase; D009601:Nitroreductases