Melanin in barley: from isolation to a possibility to influence the activity of biotransformation enzymes.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F25328859%3A_____%2F24%3AN0000026" target="_blank" >RIV/25328859:_____/24:N0000026 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/62156489:43210/24:43925853

Výsledek na webu

<a href="https://nutrinet.mendelu.cz/wcd/w-rek-nutrinet/nutrinet-2024/nutrinet-2024.pdf" target="_blank" >https://nutrinet.mendelu.cz/wcd/w-rek-nutrinet/nutrinet-2024/nutrinet-2024.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.11118/978-80-7509-994-5" target="_blank" >10.11118/978-80-7509-994-5</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Melanin in barley: from isolation to a possibility to influence the activity of biotransformation enzymes.

Popis výsledku v původním jazyce

This study describes the isolation and characterization of melanin from plant matrices using a modified version of the alkaline extraction method originally described by Sava et al. (2001). Melanin was isolated from barley (variety Nudimelanocriton) and purified through a series of organic solvent treatments, acidic hydrolysis, and repeated precipitations, yielding approximately 5 mg of pure melanin from 12 g of barley grain. Isolated melanin exhibited its characteristic properties as insolubility in water, acids, and organic solvents, while being soluble in alkaline media and precipitable below pH 3. Consistent with findings from Caldas et al. (2020) and Glagoleva et Shoeva (2020), melanin samples exhibited in alkaline media a broadband almost monotonous decrease of UV/VIS absorption from initially 200 nm, with unresolved absorption band at about 270 nm, indicative of complex conjugated structures of aromatic character. Additionally, effect of melanin on cytochrome P450 1A1/2 enzyme activity was assessed in HepG2 cells using 7-ethoxyresorufin Odealkylation and high-performance liquid chromatography. Melanin at three concentrations (10 µg/mL, 1 µg/mL and 0.1 µg/mL) did not significantly induce cytochrome P450 1A1/2 enzyme activity (in contrast to CYP1A1/2 potent inducer, 2,3,7,8-tetrachlordibenzodioxin resulting in a nearly sixtyfold increase). These findings contribute to understanding the physicochemical properties of barley-derived melanin and its interaction with hepatic enzymes of xenobiotic biotransformation (as CYP1A1/2).

Název v anglickém jazyce

Melanin in barley: from isolation to a possibility to influence the activity of biotransformation enzymes.

Popis výsledku anglicky

This study describes the isolation and characterization of melanin from plant matrices using a modified version of the alkaline extraction method originally described by Sava et al. (2001). Melanin was isolated from barley (variety Nudimelanocriton) and purified through a series of organic solvent treatments, acidic hydrolysis, and repeated precipitations, yielding approximately 5 mg of pure melanin from 12 g of barley grain. Isolated melanin exhibited its characteristic properties as insolubility in water, acids, and organic solvents, while being soluble in alkaline media and precipitable below pH 3. Consistent with findings from Caldas et al. (2020) and Glagoleva et Shoeva (2020), melanin samples exhibited in alkaline media a broadband almost monotonous decrease of UV/VIS absorption from initially 200 nm, with unresolved absorption band at about 270 nm, indicative of complex conjugated structures of aromatic character. Additionally, effect of melanin on cytochrome P450 1A1/2 enzyme activity was assessed in HepG2 cells using 7-ethoxyresorufin Odealkylation and high-performance liquid chromatography. Melanin at three concentrations (10 µg/mL, 1 µg/mL and 0.1 µg/mL) did not significantly induce cytochrome P450 1A1/2 enzyme activity (in contrast to CYP1A1/2 potent inducer, 2,3,7,8-tetrachlordibenzodioxin resulting in a nearly sixtyfold increase). These findings contribute to understanding the physicochemical properties of barley-derived melanin and its interaction with hepatic enzymes of xenobiotic biotransformation (as CYP1A1/2).

Druh

D - Stať ve sborníku

CEP obor

—

OECD FORD obor

40401 - Agricultural biotechnology and food biotechnology

Projekt

<a href="/cs/project/QL24010230" target="_blank" >QL24010230: Barevná pšenice a ječmen – výzva pro budoucnost</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

NutriNET 2024

ISBN

978-80-7509-994-5

ISSN

—

e-ISSN

—

Počet stran výsledku

15

Strana od-do

22-36

Název nakladatele

Mendelova univerzita v Brně

Místo vydání

Brno

Místo konání akce

Brno

Datum konání akce

9. 4. 2024

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

—