Complexation of dragon fruit peels-derived betacyanin with proteins: Thermal stabilities and binding mechanisms of betacyanin-protein complexes aimed as natural food colorants
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Author list: Mamu, Y.; Ngamwonglumlert, L.; Devahastin, S.; Chiewchan, N.
Publisher: Elsevier
Publication year: 2025
Journal: Food Chemistry (0308-8146)
Volume number: 496
ISBN: 9783540699330; 9781619421257
ISSN: 0308-8146
eISSN: 1873-7072
Languages: English-Great Britain (EN-GB)
Abstract
Soy protein isolate (SPI) and casein (CP) were used for betacyanin (BC) stabilization over 60–120 °C. Fluorescence spectroscopy reveals efficient complexation at BC:SPI and BC:CP ratios of 1:1.37 and 1:1.23 ( w /w). At 60 °C/40 min, betanin retention was 65.33 ± 1.06% (BC), 71.18 ± 1.91% (BC-SPI) and 73.5 ± 0.91% (BC-CP), while at 100 °C/20 min, the values dropped to 11.78 ± 0.50%, 34.19 ± 1.32% and 38.07 ± 1.73%. SPI was more protective at 60–80 °C, whereas CP outperformed SPI at 100 °C and during prolonged heating. BC-protein complexes exhibited increased α-helix and random coil contents, implying improved thermal stability and adaptability of proteins. Molecular docking simulation reveals strong binding affinities of BC to β-conglycinin and β-casein. Molecular dynamics simulation shows that at 100 °C, SPI maintains compact BC binding, whereas CP undergoes conformational change; the former thus provides BC protection yet exhibiting reduced stability under prolonged heating. These findings demonstrate that protein structural type plays crucial role in thermal protection of BC. © 2025 Elsevier Ltd.
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