Månsson M O, Mattiasson B, Gestrelius S, Mosbach K
Biotechnol Bioeng. 1976 Aug;18(8):1145-59. doi: 10.1002/bit.260180810.
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.
使用几种不同的偶联方法将各种黄素、黄素单核苷酸（FMN）、黄素腺嘌呤二核苷酸（FAD）和吖啶黄素固定到琼脂糖上。唯一稳定到足以进行深入研究的产物是与环氧取代的琼脂糖偶联的吖啶黄素。研究了其对烟酰胺腺嘌呤二核苷酸（磷酸）（NAD(P)H）的非酶氧化能力，与游离吖啶黄素相比，观察到其比活性为25%。还原型吖啶黄素在空气中会立即自动再氧化，因此可以重复使用。结果表明，吖啶黄素-琼脂糖制剂在包括乳酸脱氢酶（LDH）、乙醇脱氢酶（ADH）、苹果酸脱氢酶（MDH）、丙氨酸脱氢酶（alaDH）和谷氨酸脱氢酶（GDH）在内的多种不同脱氢酶系统中作为NAD(P)H氧化剂发挥作用。从而显著减少了此类系统高产物形成所需的昂贵辅酶的用量。
