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Comparison of α-acetolactate synthase and α-acetolactate decarboxylase in Lactococcus spp. and Leuconostoc spp
Cell-free extracts of Leuconostoc and Lactococcus species were tested for their alpha -acetolactate synthase and alpha -acetolactate decarboxylase activities. In Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. mesenteroides and Leuconostoc lactis, the Km of alpha -acetola...
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Published in: | Biotechnology letters 1994-01, Vol.16 (3), p.257-262 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | Cell-free extracts of Leuconostoc and Lactococcus species were tested for their alpha -acetolactate synthase and alpha -acetolactate decarboxylase activities. In Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. mesenteroides and Leuconostoc lactis, the Km of alpha -acetolactate synthase for pyruvate was close to 10 mM whereas it was 30 mM in Lactococcus lactis subsp. lactis biovar. diacetylactis. The Km of alpha -acetolactate decarboxylase for alpha -acetolactic acid was very low (0.3 mM) in Leuconostoc species in comparison to Lactococcus lactis subsp. lactis biovar. diacetylactis (60 mM). In the latter bacterium, alpha -acetolactate decarboxylase showed a sigmoidal dependence upon alpha -acetolactic acid and was activated by the three branched-chain amino acids: leucine, isoleucine and valine. |
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ISSN: | 0141-5492 1573-6776 |
DOI: | 10.1007/BF00134622 |