Comparison of ?-acetolactate synthase and ?-acetolactate decarboxylase in Lactococcus spp. and Leuconostoc spp. | Zendy

Christophe Monnet | Zendy; Vincent Phalip | Zendy; P. Schmitt | Zendy; C. Divi�s | Zendy

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

Author(s) -

Christophe Monnet,

Vincent Phalip,

P. Schmitt,

C. Divi�s

Publication year - 1994

Publication title -

biotechnology letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.548

H-Index - 107

eISSN - 1573-6776

pISSN - 0141-5492

DOI - 10.1007/bf00134622

Subject(s) - lactococcus lactis , leuconostoc mesenteroides , lactococcus , leuconostoc , acetolactate synthase , biology , biovar , biochemistry , microbiology and biotechnology , food science , bacteria , lactic acid , enzyme , fermentation , lactobacillus , genetics , gene

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

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