Lactate and acetate production in Listeria innocua


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Abstract

Listeria innocua NCTC 11289 was grown aerobically in continuous culture in defined media at 30°C. Both acetate and lactate were produced, the proportion of acetate decreased with increasing dilution rate. Enzymatic analysis showed lactate dehydrogenase was activated 10-fold by fructose-1,6-bisphosphate. The presence of phosphate acetyltransferase and acetate kinase but not pyruvate oxidase was detected, suggesting the sequential action of phosphate acetyltransferase and acetate kinase to produce acetate from acetyl CoA via acetylphosphate.

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