Purification and properties of the α-acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118

α-Acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118 was expressed at low levels in cell extracts and was also unstable. The purification was carried out from E. coli in which the enzyme was expressed 36-fold higher. The specific activity was 24-fold enhanced after purificati...

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Bibliographic Details
Published in:FEBS letters 1994-08, Vol.351 (1), p.95-99
Main Authors: Phalip, Vincent, Monnet, Christophe, Schmitt, Philippe, Renault, Pierre, Godon, Jean-Jacques, Diviès, Charles
Format: Article
Language:English
Subjects:
ALDC, α-acetolactate decarboxylase
BCAA, branched-chain amino acids
Branched-chain amino acids
Carboxy-Lyases - genetics
Carboxy-Lyases - isolation & purification
Carboxy-Lyases - metabolism
Chromatography, Gel
Cloning, Molecular
EDTA, ethylenediaminetetraacetic acid
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Escherichia coli
Kinetics
Lactococcus
Lactococcus lactis - enzymology
Lactococcus lactis lactis
LDH, lactate dehydrogenase
Life Sciences
Recombinant Proteins
SDS-PAGE, sodium dodecyl sulphate polyacrylamide gel electrophoresis
α-Acetolactate decarboxylase
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Summary:α-Acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118 was expressed at low levels in cell extracts and was also unstable. The purification was carried out from E. coli in which the enzyme was expressed 36-fold higher. The specific activity was 24-fold enhanced after purification. The main characteristics of α-acetolactate decarboxylase were: (i) activation by the three branched chain amino acids leucine, valine and isoleucine; (ii) allosteric properties displayed in absence and Michaelis kinetics in the presence of leucine. The enzyme is composed of six identical subunits of 26,500 Da.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(94)00820-5