Abstract
5-Keto-d-gluconate reductase (EC 1.1.1.69) was purified and crystallized for the first time from cell-free extract of Gluconobacter suboxydans IFO 12528. Purification of the enzyme was successfully performed by column chromatography on DEAE-Sephadex A–50, blue-dextran Sepharose 4B, followed by pH gradient chromatography on DEAE-Sephadex A–50. The enzyme was purified about 1200-fold with an overall yield of 40%. The enzyme was much stabilized against heating and storage by adding either d-gluconate or 5-keto-d-gluconate. 2-Keto-d-gluconate had no effect to stabilize the enzyme and the enzyme was confirmed to be a different entity from 2-keto-d-gluconate reductase stabilized by gluconate or 2-keto-d-gluconate but not 5-keto-d-gluconate. It was also confirmed with crystalline enzyme that 5-keto-d-gluconate reductase is considered to have a function to reduce intracellular 5-keto-d-gluconate to d-gluconate in combination with regeneration of NADP.
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