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Purification and properties of a malolactic enzyme from Leuconostoc oenos ATCC 23278

✍ Scribed by Pascal Naouri; Patrice Chagnaud; Dr. Alain Arnaud; Pierre Galzy

Publisher
John Wiley and Sons
Year
1990
Tongue
English
Weight
408 KB
Volume
30
Category
Article
ISSN
0233-111X

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✦ Synopsis

Abstract

The malolactic enzyme of Leuconostoc ocnos ATCC 23278 was purified 136fold. The molecular weight was estimated at 132,000 when determined by gel filtration. The enzyme contained two identical subunits (M~w~ = 66,000 using sodium dodecyl sulfate gel electrophoresis). The malolactic enzyme catalyzes the NAD^+^‐ and Mn^+^‐dependent reaction L‐malate → L‐lactate + CO~2~. The apparent K~m~ values for malic acid, NAD^+^, and Mn^2+^ were 17 mM, 0.044 mM, and 0.017 mM, respectively. The optimal pH and the optimal temperature for activity were 5.0, and 37 °C, respectively and the isoelectric point was pH 4.30. L‐lactate and ethanol were non‐competitive inhibitors, whereas succinate, citrate, and D‐tartrate showed competitive type inhibitions.

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