Summary
Cell-free extracts of Leuconostoc and Lactococcus species were tested for their α-acetolactate synthase and α-acetolactate decarboxylase activities. In Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. mesenteroides and Leuconostoc lactis, the Km of α-acetolactate synthase for pyruvate was close to 10 mM whereas it was 30 mM in Lactococcus lactis subsp. lactis biovar. diacetylactis. The Km of α-acetolactate decarboxylase for α-acetolactic acid was very low (0.3 mM) in Leuconostoc species in comparison to Lactococcus lactis subsp. lactis biovar. diacetylactis (60 mM). In the latter bacterium, α-acetolactate decarboxylase showed a sigmoidal dependance upon α-acetolactic acid and was activated by the three branchedchain amino acids: leucine, isoleucine and valine.
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Monnet, C., Phalip, V., Schmitt, P. et al. Comparison of α-acetolactate synthase and α-acetolactate decarboxylase in Lactococcus spp. and Leuconostoc spp.. Biotechnol Lett 16, 257–262 (1994). https://doi.org/10.1007/BF00134622
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DOI: https://doi.org/10.1007/BF00134622