SummaryCitrate stimulated growth, totally induced citrate lyase, partly induced acetolactate synthase activity and partly repressed both diacetyl and acetoin reductases inLeuconostoc lactisNCW1. Similar results were obtained with 2 other leuconostocs and a heterofermentative lactobacillus. In 2 of the 3 leuconostocs tested, diacetyl reductase and acetoin reductase were NADPH specific, while in the 2 heterofermentative lactobacilli, they were NADH specific.

The relationship between acetoin production and citrate utilization in Leuconostoc lactis NCW1 was studied. In a complex medium the organism utilized citrate at neutral pH (initial pH, 6.3) and at acid pH (initial pH, 4.5) but produced nine times more acetoin at the latter pH. In resting cells the utilization of citrate was optimum at pH 5.3. Production of acetoin as a function of citrate utilization increased as the pH decreased, and at pH 4.3 all of the citrate utilized was recovered as acetoin. Glucose (10 mM) and lactose (10 mM) markedly stimulated citrate utilization but totally inhibited acetoin production in glucose- and lactose-grown cells. Addition of glucose to cells actively metabolizing citrate caused an immediate increase in citrate uptake and a reduction in the level of acetoin. The apparent K m values of lactic dehydrogenase for pyruvate were 1.05, 0.25, and 0.15 mM at pH 7.5, 6.5, and 5.0, respectively. Several heterofermentation intermediates inhibited α-acetolactate synthetase and decarboxylase activities. The implications of these results in regulating acetoin formatin are discussed.