Purification and Characterization of Lactate Dehydrogenase(LDH) from the Leavening Bacterium Enterobacter cloacae GAO.
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<I>Enterobacter cloacae</I> GAO, a leavening bacterium, was studied for its assimilation of organic acids contained in a culture broth.<I>E. cloacae</I> GAO produced lactic acid and formic acid therefore, the lactate dehydrogenase (LDH) of <I>E. cloacae</I> GAO may affect the production of hydrogen gas by the bacterium. We investigated the purification and characteristics of the lactate dehydrogenase from <I>E. cloacae</I> GAO. The last purification step resulted in the specific activity of the enzyme being increased 48.5-fold with a yield of 4.6%. The molecular weight of the purified enzyme was approximately 115, 000 by gel filtration, being composed of four subunits each with a molecular weight 31, 000 as evaluated by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme activity were 7.5 and 30°C, respectively. The lactate dehydrogenase was stable at 40°C and between pH 7 and 9, and the enzyme activity was strongly inhibited by Cu<SUP>2+</SUP> and Mn<SUP>2+</SUP>. The enzyme predominantly contained glutamic acid in its amino acid composition.
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