Abstract
Regeneration of nicotinamide adenine dinucleotide phosphate (NADP) from its reduced form (NADPH) was performed in a matrix-bound form by an electrolytic method. NADP was immobilized to alginic acid. No significant loss of coenzymic function was induced by the immobilization of NADP on the matrix. Bound NADP was soluble in water. Glucose-6-phosphate dehydrogenase (G-6-PDH) was taken as a model system of coenzyme requiring enzyme. G-6-PDH immobilized on alumina particles was coupled with the soluble form of bound NADP in a fluidized bed type of reactor. The enzymatically reduced coenzyme was electrolytically oxidized in the coenzyme regenerator of NADP from NADPH, which was found to cause no harmful loss of coenzymic function.
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