3-4-dihydroxyphenylpropionic-acid and protocatechuic-acid

In this study, ten strains of Lactobacillus were used to assess the in vitro metabolism of elderberry juice polyphenols. Total polyphenolic compounds increased after starter addition, especially with three L. rhamnosus and one L. plantarum strains, of dairy origin: quercetin-3-O-rutinoside was the most abundant compound (from 39.02 ± 5.28 to 127.56 ± 11.34 µg/mL) and hydroxycinnamic acids, flavonols and anthocyanins reached the highest amounts. When L. plantarum were used phenyllactic acids presented a value of 7.05 ± 2.38 µg/mL, while in the other samples it was around 5.56 ± 1.65 µg/mL. Hydroxycinnamic and hydroxybenzoic acids were subjected to lactic acid bacteria metabolism: caffeic and protocatechuic acids were consumed during fermentation while dihydrocaffeic acid and catechol were produced. Anthocyanins increased in a strain-specific way. So, by this study we highlighted that dairy strains can produced (phenyllactic acids), modified (hydroxycinnamic acids) or increased (flavonols glycosides and anthocyanins) phenolic compounds.

Topics: Anthocyanins; Caffeic Acids; Coumaric Acids; Fermentation; Flavonols; Fruit and Vegetable Juices; Glycosides; Hydroxybenzoates; Lactobacillus; Polyphenols; Sambucus

Binding affinities to lactoperoxidase (LPO) of a homologous series of substituted catechol(amine)s [such as catechol, 4-methylcatechol, 3,4-dihydroxybenzoic acid, 3,4-dihydroxyphenylacetic acid, 3-(3,4-dihydroxyphenyl)propionic acid; dopamine, noradrenaline, adrenaline; L-3,4-dihydroxyphenylalanine] were studied by UV-visible spectroscopy and docking simulations. Dissociation constant (Kd) values were calculated by direct fitting of the experimental data and fall in a range of 3-95 mM. Thermodynamic parameters are comparable with those reported for the interaction of LPO with p-substituted phenols, suggesting a similar general mode of binding. Furthermore, the relative contributions to binding energy, described by the unimolecular constant Ku, show that interaction between protein and ligands originates from a relatively large number of groups. Docking and molecular dynamics simulations, in agreement with experimental evidence, predict that the substrate is localized into the access channel in the vicinity of heme distal pocket. This channel is characterized by a hydrophobic patch (six Phe residues) and by a charged contribution (two Glu and one His residues). All of the substrates, except caffeic acid, may approach the protein active site. Positively charged Arg372 acts as a gate above the heme distal pocket and seems to address substrate orientation in relation to the side-chain terminal group.

Topics: 3,4-Dihydroxyphenylacetic Acid; Animals; Caffeic Acids; Catalytic Domain; Catecholamines; Cattle; Computer Simulation; Dihydroxyphenylalanine; Dopamine; Hydrogen-Ion Concentration; Hydroxybenzoates; Lactoperoxidase; Models, Molecular; Norepinephrine; Protein Conformation; Spectrophotometry, Ultraviolet; Thermodynamics