Tyrosine decarboxylase activity of Lactobacillus brevis IOEB 9809 isolated from wine and L. brevis ATCC 367

Tyrosine decarboxylase from Lactobacillus brevis: soluble expression and characterization.

Tyrosine decarboxylase (TDC, EC 4.1.1.25) is an enzyme that catalyzes the decarboxylation of l-tyrosine to produce tyramine and CO2. In this study, a 1881-bp tdc gene from Lactobacillus brevis was cloned and heterologously expressed in Escherichia coli BL21 (DE3). Glucose was discovered to play an important role in the soluble expression of rLbTDC. After optimization, recombinant TDC (rLbTDC) w...

Glutamate decarboxylase from Lactobacillus brevis: activation by ammonium sulfate.

In this study, the glutamate decarboxylase (GAD) gene from Lactobacillus brevis IFO12005 (Biosci. Biotechnol. Biochem., 61, 1168-1171 (1997)), was cloned and expressed. The deduced amino acid sequence showed 99.6% and 53.1% identity with GAD of L. brevis ATCC367 and L. lactis respectively. The His-tagged recombinant GAD showed an optimum pH of 4.5-5.0, and 54 kDa on SDS-PAGE. The GAD activity a...

cloning of glutamate decarboxylase and production of γ-aminobutyric acid from lactobacillus brevis

Pyruvate metabolism in Lactobacillus brevis.

The pyruvate metabolism of LactobaciUus plantarum and Latobacillus arabino8su, which according to Bergey (1948) are identical organisms, has been studied by Rowatt (1951) and Nossal (1952). Both these homofermentative lactobacilli were shown to form 3-hydroxybutan-2-one (acetoin) as the main product of their pyruvate metabolism. No one appears to have studied the metabolism of pyruvate by any o...

1,3-Propanediol:NAD+ oxidoreductases of Lactobacillus brevis and Lactobacillus buchneri.

In the cofermentation of glycerol with a sugar by Lactobacillus brevis and Lactobacillus buchneri, a 1,3-propanediol:NAD+ oxidoreductase provides an additional method of NADH disposal. The enzyme has been purified from both L. brevis B22 and L. buchneri B190 and found to have properties very similar to those reported for the enzyme from Klebsiella pneumoniae. The enzymes required Mn2+ and are p...