Enzymatic Studies on the Formation of 5-Ketogluconic Acid by Acetobacter suboxydans

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Abstract
The cells of A. suboxydans IFO 3432 were ground with A12O3 in 0.01 [image] tris buffer (pH 7.4), the centrifuged supernatant fractionated by (NH4)2 SO4 (0.4[long dash]0.7 saturation), treated with acrinol and charcoal and the filtrate fractionated by (NH4)2 SO4 (0.5[long dash]0.7 saturation) and with acetone (35[long dash]50%). The preparation possessed glucose dehydrogenase purified about 20 fold was free of 5-ketogluconic acid reductase. The enzyme required triphosphopyridine-nucleotide (TPN) for substrate (glucose and mannose) oxidation at optimum pH of 8.5, to yield [delta]-glucono- and [delta]-manno-lactones. The enzyme catalyzed the reduction of gluconic acid in the presence of TPNH2 and [delta]-gluconolactone.

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