PT  - JOURNAL ARTICLE
AU  - F. Radler
AU  - J. Zorg
TI  - Characterization of the Enzyme Involved in Formation of 2-Butanol from <em>meso</em>-2,3-Butanediol by Lactic Acid Bacteria
AID  - 10.5344/ajev.1986.37.3.206
DP  - 1986 Jan 01
TA  - American Journal of Enology and Viticulture
PG  - 206--210
VI  - 37
IP  - 3
4099  - http://www.ajevonline.org/content/37/3/206.short
4100  - http://www.ajevonline.org/content/37/3/206.full
SO  - Am J Enol Vitic.1986 Jan 01; 37
AB  - Strains of Lactobacillus brevis originally isolated from spoiled wine reduced meso-2,3-butanediol to 2-butanol. This reaction was initiated by dehydration of the diol to methyl ethyl ketone, that acted as hydrogen acceptor during the joint fermentation of glucose to CO2, lactate, acetate, and ethanol. The diol dehydrase catalyzing the dehydration of meso-2,3-butanediol to methyl ethyl ketone was purified to electrophoretic homogeneity. The enzyme reacted with 1,2-propanediol, glycerol, and meso-2,3-butanediol. The corresponding Km values were 0.7 mM, 5.5 mM, and 34.0 mM, respectively. The dehydrase showed optimum activity at pH 7.0 and at 30°C. It was activated by ammonium and potassium ions and inhibited by lithium, sodium, magnesium, and manganese ions. The meso-butanediol dehydrase showed the same characteristics as the diol dehydrase from Lactobacillus brevis that has been isolated previously and is obviously identical to this enzyme. The meso-2,3-butanediol dehydrase had a relative molecular weight (Mr) of about 230 000 daltons and consisted of four different subunits.