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The kinetics of lactate dehydrogenase from Leuconostoc lactis NCW1 were studied. The pH optimum for the enzyme depended on the concentration of pyruvate used in the assay and the enzyme displayed an ordered mechanism with respect to substrate binding. The Km for pyruvate and NADH and the Vmax of the enzyme decreased 20–, 30– and 6-fold respectively as the pH decreased from 8·0 to 5·0. No activators were found and none of the intermediates of the phosphoketolase pathway tested inhibited the enzyme. ATP, ADP, GTP and NAD+ were inhibitory. The intracellular volume (Volin) and intracellular pH (pHin) decreased as the extracellular pH (pHex) decreased. Co-metabolism of citrate and glucose affected the Volin but did not affect the pHin, which decreased by 0·6 units per unit change in pHex; at pH 7·0, the pHin and pHex were equal. The results suggest that pHin may play a role in determining the production of diacetyl and acetoin at low pH by Leuconostoc.
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