Effect of preheat treatment of milk proteins on their interactions with cyanidin-3-O-glucoside
He, Wenjia (2018-07-10)
Effect of preheat treatment of milk proteins on their interactions with cyanidin-3-O-glucoside
He, Wenjia
(10.07.2018)
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Turun yliopisto
Tiivistelmä
Anthocyanins are a group of natural colorants with bright colors, water solubility and non-toxicity. However, they have poor stability during food processing and storage which limits their commercial applications. Previous studies indicated the need to study the binding of anthocyanins and preheated proteins. Hence, in this study, we characterized the interaction between one common anthocyanin, cyanidin-3-O-glucoside (C3G) and preheated milk proteins especially β-lactoglobulin (β-Lg) and β-casein (β-CN).
The effects of C3G and preheat treatment on the structural conformation of milk proteins were studied by Fourier transform infrared spectra and Fluorescence quenching spectroscopy. We used HPLC to analyze the remaining anthocyanins and their stability.
According to our findings, hydrogen bonding and hydrophobic interaction dominated the binding between C3G and β-Lg whereas the major forces of C3G and β-CN were hydrogen bonding and Van der Waals force. Preheat treatment of milk proteins did not alter the major force with C3G, however, the affinity of binding changed with increasing preheat temperature. The highest affinity between milk proteins and C3G was observed at 85°C preheated β-Lg at pH 6.3. The conformation of both β-Lg and β-CN were altered by the binding of C3G, with a reduction of α-helix and β-sheet and an increase of random coil and turn structures. This result provided an important information on the binding of native and preheated milk proteins and C3G and its effect on the stability of C3G.
The effects of C3G and preheat treatment on the structural conformation of milk proteins were studied by Fourier transform infrared spectra and Fluorescence quenching spectroscopy. We used HPLC to analyze the remaining anthocyanins and their stability.
According to our findings, hydrogen bonding and hydrophobic interaction dominated the binding between C3G and β-Lg whereas the major forces of C3G and β-CN were hydrogen bonding and Van der Waals force. Preheat treatment of milk proteins did not alter the major force with C3G, however, the affinity of binding changed with increasing preheat temperature. The highest affinity between milk proteins and C3G was observed at 85°C preheated β-Lg at pH 6.3. The conformation of both β-Lg and β-CN were altered by the binding of C3G, with a reduction of α-helix and β-sheet and an increase of random coil and turn structures. This result provided an important information on the binding of native and preheated milk proteins and C3G and its effect on the stability of C3G.