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Continuous production of NADP by immobilized Achromobacter aceris cells
Author(s) -
Uchida Tomofumi,
Watanabe Taizo,
Kato Jyoji,
Chibata Ichiro
Publication year - 1978
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.260200208
Subject(s) - nad+ kinase , substrate (aquarium) , biochemistry , chemistry , enzyme , nicotinamide adenine dinucleotide , achromobacter , chromatography , immobilized enzyme , adenosine triphosphate , microbiology and biotechnology , pseudomonas , biology , bacteria , ecology , genetics
Several microorganisms having higher nicotinamide adenine dinucleotide kinase (NAD kinase, EC 2.7.1.23) activity were immobilized into polyacrylamide gel lattices. The enzyme activity yield by immobilization was highest in Achromobacter aceris AKU 0120. By the incubation of the immobilized A. aceris cells at pH 4.0, the NAD kinase activity increased and the adenosine triphosphate(ATP)‐degradation activity disappeared completely. Enzymic properties of the immobilized A. aceris cells were investigated and compared with those of intact cells. The optimal pH and the optimal temperature of immobilized cells were the same as those of intact cells. Immobilized cell NAD kinase was more stable than that of intact cells. The operational half‐life of immobilized cells was 20 days when the substrate solution was passed through a column packed with immobilized cells at a flow rate which gives a space velocity (SV) of 0.1 hr −1 at 37°C. On the other hand, the half‐life of the intact cells was only 6 hr.