6533b82ffe1ef96bd1295297

RESEARCH PRODUCT

Comparison of α-acetolactate synthase and α-acetolactate decarboxylase in Lactococcus spp. and Leuconostoc spp.

P. SchmittChristophe MonnetCharles DivièsV. Phalip

subject

Lactococcus[SDV]Life Sciences [q-bio]BioengineeringdiacetylactisApplied Microbiology and BiotechnologyMicrobiology03 medical and health sciencesValineLeuconostoccitrateglucose030304 developmental biology0303 health sciencesAcetolactate synthasebiology030306 microbiologyLactococcus lactisfood and beveragesGeneral Medicinebiology.organism_classificationmesenteroides subsp cremorisAcetolactate decarboxylasecarbohydrates (lipids)productslactisBiochemistryLeuconostoc mesenteroidesco-metabolismbiology.proteinbacteriaglucose;products;diacetylactis;lactis;citrate;co-metabolism;mesenteroides subsp cremorisIsoleucineBiotechnology

description

Cell-free extracts of Leuconostoc and Lactococcus species were tested for their alpha-acetolactate synthase and alpha-acetolactate decarboxylase activities. In Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. mesenteroides and Leuconostoc lactis, the Km of alpha-acetolactate synthase for pyruvate was close to 10 mM whereas it was 30 mM in Lactococcus lactis subsp. lactis biovar. diacetylactis. The Km of alpha-acetolactate decarboxylase for alpha-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, alpha-acetolactate decarboxylase showed a sigmoidal dependance upon alpha-acetolactic acid and was activated by the three branched-chain amino acids: leucine, isoleucine and valine.

10.1007/bf00134622https://hal.archives-ouvertes.fr/hal-01566301