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Comparison of α-acetolactate synthase and α-acetolactate decarboxylase inLactococcusspp. andLeuconostocspp.

✍ Scribed by C. Monnet; V. Phalip; P. Schmitt; C. Diviès


Book ID
104635544
Publisher
Springer Netherlands
Year
1994
Tongue
English
Weight
484 KB
Volume
16
Category
Article
ISSN
0141-5492

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✦ Synopsis


CeMiee extracts of tcucatrostof and &3culcpccut species were tested for their a-a&oWate syndmse and aacelolaetate dtmrboxylase activities. In ~~co~stuc meseffteroides subq. crmi3r&, Leacotwstoc mesentefoides subsp. ~senjeroldes and Leucon~~c factis, the Km of a-xetolactate synthase for pyruvate was close to 10 mM wm it was 30 mM in L~r~acc~ luctis subsp. lactis boom. ~~e~~actjs. The Km of a-acetolactate decarboxylase for a-xetoiactic acid was very low {ft.3 mM) in Letwaastoc specks in can-to Lactococcas luctis s&p. luctis biovx. diacery~uctis (60 mM). In the latter bacterium, a-acetolactttte decarboxytase showed a sigmoidal depe&mce upar a-xetolactic acid and W(IS activated by the thne bmncbuichain amino acids: kucine, isoleucine and v&e.

Luctacmms iactis subsp. fact& biovtu. diacetylacts and Leuconusroc spp. am used in the dairy industry for the production of diacetyl duting the fe~n~i~ of milk. Citmte is the pncutsa of C, {acetoin, diacetyl and 23-


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