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).

Effect of Fermented Soy Beverage on Equol Production by Fecal Microbiota.

Soy consumption is associated with health benefits, mainly linked to the ability of the intestinal microbiota to metabolize the glycosylated isoflavones into more bioactive compounds, such as equol. Because INIA P815 is able to efficiently deglycosylate daidzin into daidzein, the aim of this work was to confirm the influence of soy beverages fermented by INIA P815 for enhancing equol production by fecal microbiota. Firstly, fecal samples from 17 participants were characterized in vitro, and we observed that 35.

Production of recombinant glycosidases fused with Usp45 and SpaX to avoid the purification and immobilization stages.

The elucidation of the physicochemical properties of glycosidases is essential for their subsequent technological application, which may include saccharide hydrolysis processes and oligosaccharide synthesis. As the application of cloning, purification and enzymatic immobilization methods can be time consuming and require a heavy financial investment, this study has validated the recombinant production of the set of Lacticaseibacillus rhamnosus fucosidases fused with Usp45 and SpaX anchored to the cell wall of Lacticaseibacillus cremoris subsp cremoris MG1363, with the aim of avoiding the purification and stabilization steps. The cell debris harboring the anchored AlfA, AlfB and AlfC fucosidases showed activity against p-nitrophenyl α-L-fucopyranoside of 6.