Carlsberg Research Communications

, 50:73

Purification of α-acetolactate decarboxylase from Lactobacillus casei DSM 2547

Authors

  • Anne M. Rasmussen
    • Department of ChemistryCarlsberg Laboratory
  • Richard M. Gibson
    • Department of ChemistryCarlsberg Laboratory
  • Sven Erik Godtfredsen
    • Department of ChemistryCarlsberg Laboratory
  • Martin Ottesen
    • Department of ChemistryCarlsberg Laboratory
Article

DOI: 10.1007/BF02907138

Cite this article as:
Rasmussen, A.M., Gibson, R.M., Godtfredsen, S.E. et al. Carlsberg Res. Commun. (1985) 50: 73. doi:10.1007/BF02907138

Abstract

α-Acetolactate decarboxylase has been purified to homogeneity, by fast protein liquid chromatography and high performance elution chromatography, from a partially purified α-acetolactate decarboxylase preparation from Lactobacillus casei DSM 2547. The pure enzyme exhibited a specific activity of 375 kU·mg−1 and exerted its optimal activity at pH 4.5 to 5.0 and at a temperature of 40°C. Its isoelectric point was estimated to pH 4.7 and its molecular weight was found to be 48,000. The enzyme was inhibited by o-phenanthroline and could be partially reactivated by zinc ions. An HPLC method for the determination of α-acetolactate is described.

Keywords

α-acetolactateα-acetolactate decarboxylaseacetoindiacetyllactic acid bacteriabeer maturationHPLC

Abbreviations

ALDC

α-acetolactate decarboxylase

AUFS

absorbance units full scale

BSA

bovine serum albumin

DSM

Deutsche Sammlung von Mikroorganismen

EDTA

ethylene diaminetetraacetic acid

HPEC

high performance exclusion chromatography

HPLC

high performance liquid chromatography

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Copyright information

© Carlsberg Laboratory 1985