Shigemi Morimoto, K. Azuma, T. Oshima
1988
Citations
0
Influential Citations
4
Citations
Journal
Journal of Fermentation Technology
Abstract
Abstract The new enzyme, propioin synthase, concerned with the formation of propioin from propionaldehyde was purified 270-fold from the crude enzyme in a yield of 28% by protamine sulfate precipitation, ammonium sulfate fractionation and G-200 gel chromatography using citrate-phosphate buffer (0.1 M Na2HPO4–0.02 M citric acid, pH 6.8, containing 0.33 mM MgSO4, 0.1 mM thiamine pyrophosphate, 2.5 mM MnSO4 and 30 mM β-mercaptoethanol). The purified enzyme was homogeneous on disc gel electrophoresis. It was most active at pH 6.8–7.0 and 37°C, and stable at pH 7–8 and below 45°C. Its activity was enhanced by FeSO4·7H2O, MnSO4, thiamine pyrophosphate, β-mercaptoethanol, MgSO4, CaCO3, and NaCl, and inhibited by AgNO3, HgCl2, CuSO4, ZnSO4, SnCl2, NH4Cl, (CH3COO)2Pb·3H2O, iodoacetic acid, FeCl3·6H2O, and (NH4)2SO4. Its molecular weight was 96,000 by sedimentation equilibrium, and 100,000 by Sephadex G-200 column chromatography.