Selection of GABA-Producing Lactic Acid Bacteria Strains by Polymerase Chain Reaction Using Novel B and C Multispecies Primers for the Development of New Functional Foods.

Gamma-aminobutyric acid (GABA) has been attributed to health-promoting properties and has received attention from the food industry as an attractive bioactive compound for the development of functional foods. Some lactic acid bacteria (LAB) produce GABA through a glutamate decarboxylase encoded by B and a glutamate/GABA antiporter encoded by C. In this study, we develop a molecular screening method based on a polymerase chain reaction able to detect those genes in different LAB species through the use of novel multispecies primers.

Production of equol, dehydroequol, 5-hydroxy-equol and 5-hydroxy-dehydroequol in soy beverages by the action of dihydrodaidzein reductase in Limosilactobacillus fermentum strains.

Equol and 5-hydroxy-equol, and their analogous compounds dehydroequol and 5-hydroxy-dehydroequol, are bioactive isoflavones formed by microbial metabolism. The aims of this work were to elucidate the formation of dehydroequol and 5-hydroxy-dehydroequol, to identify the role of dihydrodaidzein reductase (DHDR) in the production of equol, dehydroequol, 5-hydroxy-equol and 5-hydroxy-dehydroequol and to develop soy beverages enriched in these compounds through engineered lactic acid bacteria. DHDR was responsible for the production of equol and dehydroequol from dihydrodaidzein (DHD), and of 5-hydroxy-equol and 5-hydroxy-dehydroequol from dihydrogenistein (DHG), even in the absence of tetrahydrodaidzein reductase (THDR).