Production of plant-based fermented beverages possessing functional ingredients antioxidant, γ-aminobutyric acid and antimicrobials using a probiotic Lactiplantibacillus plantarum strain L42g as an efficient starter culture.

Plant-based probiotic beverages have gained increasing interest due to demand from health-conscious consumers. In this study, we aimed to isolate and screen lactic acid bacteria possessing functional properties for use as a starter culture of fermented almond and coix beverages. Lactiplantibacillus plantarum L42g isolated from fermented beef was selected.

Recombinant Expression, Purification and Characterization of Pyridoxal 5'-phosphate Synthase from sp. H6a, Thermophilic Bacterium Producing Extracellular Vitamin B6.

Background: Pyridoxal 5' -phosphate synthase (PLPS) is present in deoxyxylose 5'-phosphate-independent of the vitamin B6 biosynthesis pathway. This enzyme complex consists of PdxS and PdxT, which function as synthase and glutamine amidotranferase respectively to produce PLP.

Objectives: This study aimed to clone, express, and purify PLPS of  sp.

Molecular cloning, expression, and properties of an unusual aldo-keto reductase family enzyme, pyridoxal 4-dehydrogenase, that catalyzes irreversible oxidation of pyridoxal.

Microbacterium luteolum YK-1 has pyridoxine degradation pathway I. We have cloned the structural gene for the second step enzyme, pyridoxal 4-dehydrogenase. The gene consists of 1,026-bp nucleotides and encodes 342 amino acids.

An enzymatic fluorometric assay for pyridoxal with high specificity and sensitivity.

An enzymatic fluorometric assay for pyridoxal with pyridoxal dehydrogenase was developed. The detection limit was about 10 pmol: the calibration curve of pyridoxal showed high linearity (r=0.993).

Purification and characterization of pyridoxal 4-dehydrogenase from Aureobacterium luteolum.

A pyridoxal dehydrogenase was purified to homogeneity from Aureobacterium luteolum, which can use pyridoxine as a carbon and nitrogen source, and characterized. The enzyme was a dimeric protein with a subunit molecular weight of 38,000. It had several properties distinct from those of the partially purified enzyme from Pseudomonas MA-1.