Browsing by Subject "Betalain"

Now showing 1 - 4 of 4
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    Characterization of betalain-loaded liposomes and its bioactive potential in vivo after ingestion
    (Elsevier, 2022-12-09) Martínez-Rodriguez, Pedro; Guerrero-Rubio, M.Alejandra; Hernández García, Samanta; Henarejos Escudero, Paula; Gandía Herrero, Fernando; García Carmona, Francisco; Bioquímica y Biología Molecular A
    Betalains are plant pigments characterized by showing a wide range of beneficial properties for health. Its bioactive potential has been studied for the first time after its encapsulation in liposomes and subsequent administration to the animal model Caenorhabditis elegans. Phenylalanine-betaxanthin and indoline carboxylic acid-betacyanin encapsulated at concentrations of 25 and 500 μM managed to reduce lipid accumulation and oxidative stress in the nematodes. Highly antioxidant betalains dopaxanthin and betanidin were also included in the survival analyses. The results showed that phenylalanine-betaxanthin was the most effective betalain by increasing the lifespan of C. elegans by 21.8%. In addition, the administration of encapsulated natural betanidin increased the nematodes’ survival rate by up to 13.8%. The preservation of the bioactive properties of betalains manifested in this study means that the stabilization of the plant pigments through encapsulation in liposomes can be postulated as a new way for administration in pharmacological and food applications.
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    Escherichia coli protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA-extradiol-dioxygenase activity
    (Springer, 2013-05-12) Gandía Herrero, Fernando; García Carmona, Francisco; Bioquímica y Biología Molecular "A"
    Betalamic acid is the structural unit of all the natural pigments betalains. These are nitrogen-containing water soluble compounds with high colorant and bioactive properties, characteristic of plants of the order Caryophyllales. The formation of betalamic acid from the precursor amino acid 3,4-dihydroxy-L-phenylalanine (L-DOPA) by the enzyme 4,5- DOPA-extradiol-dioxygenase was supposed to be restricted to plants of this order and two fungal species. Here, the first case of betalamic acid formation by an enzyme other than eukaryotes is reported with a homolog enzyme from Escherichia coli. The protein YgiD has been cloned, expressed, and purified to carry out its molecular and functional characterization. The enzyme was obtained as a monomeric active protein with a molecular mass of 32 kDa characterized by chromatography, electrophoresis, and MALDI-TOF analysis. Enzyme kinetic properties are characterized in the transformation of the relevant substrate L-DOPA. Reaction was analyzed spectrophotometrically and by HPLC-DAD, electrospray ionization mass spectrometry, and time-of-flight mass spectrometry
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    Inactivation of lipoxygenase and cyclooxygenase by natural betalains and semi-synthetic analogues
    (Elsevier, 2014-01-13) Vidal, Pedro J.; Gandía Herrero, Fernando; López Nicolás, José Manuel; García Carmona, Francisco; Bioquímica y Biología Molecular "A"
    Betalains are natural pigments characteristic of plants of the order Caryophyllales. In this work, the role of betalains in the anti-inflammatory activity described for plant extracts is analysed in terms of the inactivation of the enzymes involved in the biochemical response (lipoxygenase and cyclooxygenase). Pure natural betalains and semi-synthetic analogues are demonstrated to promote a significant reduction of the enzymes activity. Reactions were followed spectrophotometrically and by HPLC-DAD. Phenethylamine-betaxanthin was the most potent in the inactivation of cyclooxygenase, with a reduction of 32% of the control activity at 125 lM, while the natural pigment betanidin and a betalain analogue derived from indoline resulted as the most potent inactivators of lipoxygenase, with IC50 values of 41.4 and 40.1 lM, respectively. Molecular docking studies revealed that betalains interact with the lipoxygenase amino acids involved in substrate binding and with Tyr-385 and Ser-530 close to the yclooxygenase active site, interfering in enzyme catalysis.
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    Structural implications on color, fluorescence, and antiradical activity in betalains
    (2010-05-14) Escribano Cebrián, Josefa; Gandía Herrero, Fernando; García Carmona, Francisco; Departamento de Bioquímica y Biología Molecular A; Facultad de Veterinaria
    Betalains are water-soluble pigments with high antiradical capacity which bestow bright colors on Xowers and fruits of most plants of the order Caryophyllales. They are classiWed as betacyanins, exhibiting a violet coloration, and betaxanthins, which exhibit yellow coloration. Traditionally, betalains have been defined as condensation products of betalamic acid with different amines and amino acids, but the implication of the pigment structure for their properties has not been investigated. This paper explores different structural features of the betalains, revealing the clues for the switch from yellow to violet color, and the loss of fluorescence. A relevant series of 15 betalain-related compounds (both natural and novel semisynthetic ones) is obtained and characterized by chromatography, UV-vis spectrophotometry, fluorescence, and electrospray ionization mass spectroscopy. Antiradical properties of individual pure compounds in a broad pH range are studied under the ABTS•+ radical assay. Relevance of specific bonds is studied, and diferences between betaxanthins and betacyanins are used to explore in depth the structure–antiradical activity relationships in betalains.