The level of pyruvate-formate lyase controls the shift from homolactic to mixed-acid product formation in Lactococcus lactis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-03

AUTHORS

Rix C. Melchiorsen, Væver K. Jokumsen, J. Villadsen, H. Israelsen, J. Arnau

ABSTRACT

Regulation of pyruvate-formate lyase (PFL) activity in vivo plays a central role in the shift from homolactic to mixed-acid product formation observed during the growth of Lactococcus lactis on glucose and galactose, respectively. Characterisation of L. lactis MG1363 in anaerobic batch cultures showed that the specific in vivo activity (flux) of PFL was 4-fold higher in L. lactis cells grown with galactose, compared with cells grown with glucose. The change in the PFL flux correlated with the observed variation in the PFL enzyme level, i.e. the PFL enzyme level was 3.4-fold higher in L. lactis cells grown on galactose than in those grown on glucose. To investigate whether a variation in the level of PFL was responsible for the shift in pyruvate metabolism, L. lactis strains with altered expression of pfl were constructed. The pfl gene was expressed under the control of different constitutive promoters in L. lactis MG1363 and in the PFL-deficient strain CRM40. Strains with five different PFL levels were obtained. Variation in the PFL level markedly affected the resulting end-product formation in these strains. During growth on galactose, the flux towards mixed-acid products was to a great extent controlled by the PFL level. This demonstrates that a regulated PFL level plays a predominant role in the regulation of the metabolic shift from homolactic to mixed-acid product formation in L. lactis. More... »

PAGES

338-344

Journal

TITLE

Applied Microbiology and Biotechnology

ISSUE

3

VOLUME

58

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s00253-001-0892-5

    DOI

    http://dx.doi.org/10.1007/s00253-001-0892-5

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1003470765

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11935185


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