Peer-Reviewed Journal Details
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O'Sullivan, SM,Condon, S,Cogan, TM,Sheehan, D;
2001
January
Fems Microbiology Letters
Purification and characterisation of acetolactate decarboxylase from Leuconostoc lactis NCW1
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enzyme purification decarboxylase acetoin diacetyl acetaldehyde Leuconostoc cheese LACTOCOCCUS-LACTIS ALPHA-ACETOLACTATE DIACETYL METABOLISM ACETOIN CITRATE GENES
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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. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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