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Continuous regeneration of NAD(P) + by flavins covalently bound to sepharose
Author(s) -
Månsson M. O.,
Mattiasson B.,
Gestrelius S.,
Mosbach K.
Publication year - 1976
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260180810
Subject(s) - sepharose , alcohol dehydrogenase , cofactor , glutamate dehydrogenase , biochemistry , nad+ kinase , chemistry , dehydrogenase , lactate dehydrogenase , malate dehydrogenase , oxidizing agent , flavin group , enzyme , chromatography , organic chemistry , glutamate receptor , receptor
Abstract Various flavins, FMN, FAD, and acriflavin, were immobilized to Sepharose using several different coupling methods. The only product stable enough to permit extended studies was acriflavin coupled to epoxy‐substituted Sepharose. The nonenzymic oxidizing capacity towards NAD(P)H was investigated and a 25% specific activity, compared to that of free acriflavin, was observed. The reduced acriflavin was immediately auto‐reoxidized in air and could thus be reused. It was shown that acriflavin‐Sepharose preparations function as NAD(P)H oxidizing agents in a number of different dehydrogenase systems including lactate dehydrogenase (LDH), alcohol dehydrogenase (ADH), malate dehydrogenase (MDH), alanine dehydrogenase (alaDH), and glutamate dehydrogenase (GDH). The amount of expensive coenzyme necessary for high product formation of such systems was thereby markedly reduced.