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

FEBS Letters

Schmitt, Philippe¹  Monnet, Christophe¹  Renault, Pierre²  Godon, Jean-Jacques²  Phalip, Vincent¹  Diviès, Charles¹ 

[1] Laboratoire de Microbiologie, ENS.BANA, 1 esplanade Erasme, 21000 Dijon, France;Laboratoire de Génétique Microbienne, Institut National de la Recherche Agronomique, 78352 Jouy en Josas, France

关键词: Lactococcus;    α-Acetolactate decarboxylase;    Branched-chain amino acids;    ALDC;    α-acetolactate decarboxylase;    LDH;    lactate dehydrogenase;    BCAA;    branched-chain amino acids;    SDS-PAGE;    sodium dodecyl sulphate polyacrylamide gel electrophoresis;    EDTA;    ethylenediaminetetraacetic acid;   

DOI  :  10.1016/0014-5793(94)00820-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown