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Malic acid production by an electrochemical reduction system combined with the use of diaphorase and methylviologen
Author(s) -
Maeda H.,
Kajiwara S.
Publication year - 1985
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.260270508
Subject(s) - malic acid , diaphorase , nad+ kinase , chemistry , substrate (aquarium) , malate dehydrogenase , malic enzyme , electrochemistry , electrolysis , yield (engineering) , dehydrogenase , glassy carbon , inorganic chemistry , biochemistry , nuclear chemistry , enzyme , electrode , materials science , cyclic voltammetry , biology , citric acid , ecology , metallurgy , electrolyte
A regenerating reaction combined with the use of native malate dehydrogenase, native diaphorase, methylviologen, NAD, oxalacetic acid as the substrate and lipoamide as a stabilizer was carried out in the presence of electrolysis. Consequently, malic acid was efficiently produced from oxalacetic acid in the regenerating reaction. A glassy carbon bead electrode was used as a cathode. Twenty four milliamperes were passed at a rotation speed of 500 rpm, 29.8 ± 0.3°C and −1.0 V. It was found that lipoamide has a stabilizing effect on malate dehydrogenase and diaphorase. Low concentration (50 μ M ) of NAD was also effective for the stabilization of malate dehydrogenase. NADH regeneration activity based on malic acid production rate was 4.7 U/mg of the enzyme protein of the commercial diaphorase preparation. The current efficiency was more than 74%, compared with the theoretical yield, in the presence of enough oxalacetic acid.