Complete amino acid sequence of α-acetolactate decarboxylase from Bacillus brevis

  • IB Svendsen
  • Birger Rostgaard Jensen
  • Martin Ottesen


The complete amino acid sequence of acetolactate decarboxylase (EC from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29.093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.


Beer maturation 



acetolactate decarboxylase


carboxypeptidase II from malt


carboxypeptidase Y from yeast


trifluoro acetic acid


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Copyright information

© Carlsberg Laboratory 1989

Authors and Affiliations

  • IB Svendsen
    • 1
  • Birger Rostgaard Jensen
    • 2
  • Martin Ottesen
    • 1
  1. 1.Carlsberg LaboratoryDepartment of ChemistryCopenhagen Valby
  2. 2.Novo Industry A/SBagsvaerd

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