Abstract
Anthocyanins are desirable compounds in the food industry owing to their attractive color and high biological activity; however, their poor stability remains a substantial challenge. Here, we show that low-concentration (15 mg/mL) collagen hydrolysate (CH) exhibits a potent stabilization effect on red cabbage anthocyanins (RCAs). CH extended the half-life of RCA by 6.2-fold from 40.7 to 251.1 h. Dynamic light scattering and transmission electron microscopy confirmed the formation of CH–RCA complexes, which exhibited stronger antioxidant activity than RCA alone. Ultraviolet-vis and infrared spectra demonstrated that RCA binding resulted in a more open and disordered CH structure. Centaureidin-3-O-glucoside (C3G) exhibited high affinity for CH, with a binding ratio close to 1.5:1. 1H nuclear magnetic resonance confirmed that the main interaction sites with CH were at the C3G A- and C-rings. This study clarifies how protein hydrolysates protect against anthocyanin degradation from experimental and theoretical aspects.
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