| Autor: |
O'Sullivan, Siobhán M, Condon, Seamus, Cogan, Timothy M, Sheehan, David |
| Zdroj: |
FEMS Microbiology Letters; January 2001, Vol. 194 Issue: 2 p245-249, 5p |
| Abstrakt: |
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 lactisNCW1. 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 pIof 4.2 and its activity is independent of metals or branched chain amino acids. At the optimum pH, the Kmfor 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. |
| Databáze: |
Supplemental Index |
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