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Updated: Aug 14, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Purification and characterisation of acetolactate decarboxylase from Leuconostoc lactis NCW1
S M O'Sullivan1, S Condon, T M Cogan
1Department of Biochemistry, University College Cork, Ireland.
Abstract:
A two-step strategy involving DEAE-cellulose and POROS PI anion exchange chromatography has been developed for rapid purification of acetolactate decarboxylase (ALD) from Leuconostoc lactis NCW1. This results in 5333-fold purification with a yield of 30%. Purified ALD is a dimer of 49-kDa subunits, has a pH optimum of 6.0, a pI of 4.2 and its activity is independent of metals or branched chain amino acids. At the optimum pH, the K(m) for 2-acetolactate (ALA) was found to be 1.3 mM and the turnover number was 4000 min(-1). N-terminal sequence comparison with other ALDs showed little sequence conservation in this region. Purified ALD does not catalyse direct production of diacetyl from ALA, unlike the crude extract.
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