探究乳清蛋白成分对矢车菊素-3-O-葡萄糖苷相互作用及稳定性的影响。
Exploring the effects of whey protein components on the interaction and stability of cyanidin-3-O-glucoside.
作者信息
Zhang Huimin, Ju Mengmeng, Hamid Nazimah, Ma Qianli, Shang Dansen, Jia Chengli, Xiao Yuhang, Jiang Shijing, Qiu Haoqin, Luan Wenli, Sun Aidong
机构信息
College of Biological Science and Technology, Beijing Key Laboratory of Forest Food Processing and Safety, Beijing Forestry University, Beijing, China.
Department of Food Science, Auckland University of Technology, Auckland, New Zealand.
出版信息
J Sci Food Agric. 2025 Jan 15;105(1):294-304. doi: 10.1002/jsfa.13828. Epub 2024 Aug 23.
BACKGROUND
Anthocyanins are susceptible to degradation due to external factors. Despite the potential for improved anthocyanin stability with whey protein isolate (WPI), the specific effects of individual components within WPI on the stability of anthocyanins have yet to be studied extensively. This study investigated the interaction of WPI, β-lactoglobulin (β-Lg), bovine serum albumin (BSA), and lactoferrin (LF) with cyanidin-3-O-glucoside (C3G), and also considered their effects on stability.
RESULTS
Fluorescence analysis revealed static quenching effects between C3G and WPI, β-Lg, BSA, and LF. The binding constants were 1.923 × 10 L · mol⁻¹ for WPI, 24.55 × 10 L · mol⁻¹ for β-Lg, 57.25 × 10 L · mol⁻¹ for BSA, and 1.280 × 10 L · mol⁻¹ for LF. Hydrogen bonds, van der Waals forces, and electrostatic attraction were the predominant forces in the interactions between C3G and WPI and between C3G and BSA. Hydrophobic interaction was the main binding force in the interaction between C3G and β-Lg and between C3G and LF. The binding of C3G with WPI, β-Lg, BSA, and LF was driven by different thermodynamic parameters. Enthalpy changes (∆H) were -38.76 kJ · mol⁻¹ for WPI, -17.59 kJ · mol⁻¹ for β-Lg, -16.09 kJ · mol⁻¹ for BSA, and 39.50 kJ · mol⁻¹ for LF. Entropy changes (∆S) were -67.21 J · mol⁻¹·K⁻¹ for WPI, 3.72 J · mol⁻¹·K⁻¹ for β-Lg, 37.09 J · mol⁻¹·K⁻¹ for BSA, and 192.04 J · mol⁻¹·K⁻¹ for LF. The addition of C3G influenced the secondary structure of the proteins. The decrease in the α-helix content suggested a disruption and loosening of the hydrogen bond network structure. The presence of proteins enhanced the light stability and thermal stability (stability in the presence of light and heat) of C3G. In vitro simulated digestion experiments demonstrated that the addition of proteins led to a delayed degradation of C3G and to improved antioxidant capacity.
CONCLUSION
The presence of WPI and its components enhanced the thermal stability, light stability, and oxidation stability of C3G. Preheated proteins exhibited a more pronounced effect than unheated proteins. These findings highlight the potential of preheating protein at appropriate temperatures to preserve C3G stability and bioactivity during food processing. © 2024 Society of Chemical Industry.
背景
花青素易受外部因素影响而降解。尽管乳清蛋白分离物（WPI）有可能提高花青素的稳定性，但WPI中各个成分对花青素稳定性的具体影响尚未得到广泛研究。本研究调查了WPI、β-乳球蛋白（β-Lg）、牛血清白蛋白（BSA）和乳铁蛋白（LF）与矢车菊素-3-O-葡萄糖苷（C3G）的相互作用，并考察了它们对稳定性的影响。
结果
荧光分析显示C3G与WPI、β-Lg、BSA和LF之间存在静态猝灭效应。WPI的结合常数为1.923×10 L·mol⁻¹，β-Lg为24.55×10 L·mol⁻¹，BSA为57.25×10 L·mol⁻¹，LF为1.280×10 L·mol⁻¹。氢键、范德华力和静电引力是C3G与WPI以及C3G与BSA之间相互作用的主要作用力。疏水相互作用是C3G与β-Lg以及C3G与LF之间相互作用的主要结合力。C3G与WPI、β-Lg、BSA和LF的结合由不同的热力学参数驱动。WPI的焓变（∆H）为 -38.76 kJ·mol⁻¹，β-Lg为 -17.59 kJ·mol⁻¹，BSA为 -16.09 kJ·mol⁻¹，LF为39.50 kJ·mol⁻¹。熵变（∆S）为WPI -67.21 J·mol⁻¹·K⁻¹，β-Lg 3.72 J·mol⁻¹·K⁻¹，BSA 37.09 J·mol⁻¹·K⁻¹，LF 192.04 J·mol⁻¹·K⁻¹。C3G的添加影响了蛋白质的二级结构。α-螺旋含量的降低表明氢键网络结构受到破坏并变得松散。蛋白质的存在增强了C3G的光稳定性和热稳定性（在光照和加热条件下的稳定性）。体外模拟消化实验表明，蛋白质的添加导致C3G降解延迟并提高了抗氧化能力。
结论
WPI及其成分的存在增强了C3G的热稳定性、光稳定性和氧化稳定性。预热后的蛋白质比未加热的蛋白质表现出更显著的效果。这些发现突出了在适当温度下预热蛋白质以在食品加工过程中保持C3G稳定性和生物活性的潜力。© 2024化学工业协会。
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