Purification and Properties of NAD-Linked 1, 2-Butanediol Dehydrogenase from Rhodococcus sp. strain TB-42

Abstract

1, 2-Butanediol (1, 2-BD) dehydrogenase was purified from Rhodococcus sp. strain TB-42. The activity of this enzyme was induced by 1, 2-BD and the highest activity was observed in the cells grown on 1, 2-BD as a carbon source. The native enzyme had a molecular mass of 80 kDa, and was composed of two different subunits with molecular masses of 46kDa and 43kDa. The enzyme showed a pH optimum of 10.5, and displayed the highest activity at 35-40°C. NADP could not replace NAD as an electron acceptor for the reaction. The enzyme oxidized diols with two adjacent hydroxy groups such as 1, 2-propanediol, 1, 2-BD, 2, 3-BD, and 1, 2-pentanediol except for 1, 2-ethanediol. Other diols, primary and secondary alcohols, could not be used as substrates for this enzyme.