[Purification and various properties of NADP+-dependent alcohol dehydrogenase from Acinetobacter calcoaceticus]

The constitutive NADP+-dependent alcohol dehydrogenase from Acinetobacter calcoaceticus can be accumulated about 50 fold in 3 purification steps. The end-product shows in the analytical polyacrylamide gel electrophoresis only one active enzyme band. The molecular weight of the enzyme was determined to be 235,000 by gel chromatography on Sephadex G 200, the smallest subunit shows a molecular weight of 61 000 on SDS electrophoresis. The isoelectric point is at 5.84. The KM values determined with primary aliphatic alcohols diminish in the range of the homologous order (C2--C10) with growing chain length. The KM value for hexanal is about 20 fold less than that for 1-hexanol.