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Effect of ilvBN-encoded α-acetolactate synthase expression on diacetyl production in Lactococcus lactis

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Abstract

Conversion of pyruvate to α-acetolactate, which is broken down to diacetyl and acetoin, can be catalysed by two α-acetolactate synthases in Lactococcus lactis. The enzyme encoded by the als gene (Als) has previously been shown to have a low affinity for pyruvate, which limits the formation of diacetyl. In this study we have expressed from a plasmid the ilvBN genes, which encode the other α-acetolactate synthase (IlvBN). This plasmid-directed enzyme expression provided up to 3.6-fold increased product formation in the L. lactis MG1363 and IL1403 backgrounds. Plasmid-based expression of the ilvBN genes, in an IL1403 derivative from which the leu.ilv.ald and flanking genes had been deleted, yielded up to 0.1 mM diacetyl where-as the host strain produced none. In addition, IlvBN, with a K m value of 8.3 mM, was shown to have a greater affinity for pyruvate than does Als.

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Benson, K.H., Godon, J.J., Renault, P. et al. Effect of ilvBN-encoded α-acetolactate synthase expression on diacetyl production in Lactococcus lactis . Appl Microbiol Biotechnol 45, 107–111 (1996). https://doi.org/10.1007/s002530050656

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  • DOI: https://doi.org/10.1007/s002530050656

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