Liu Qingguan, Huang Wanqing, Zhou Chunxia, Yang Sichen, Hong Jiaqi, Xie Ailin, Cui Qiang
College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China.
College of Light Industry and Food Sciences, Zhongkai University of Agriculture and Engineering, Guangzhou 510225, China.
Food Chem X. 2025 May 15;28:102563. doi: 10.1016/j.fochx.2025.102563. eCollection 2025 May.
This study delves into the feasibility of developing an intestinal delivery system for curcumin using whey protein as the wall material, employing a simple and eco-friendly (without using organic solvents) pH-induced protein-polyphenol co-assembly strategy. The results indicate that stable complex formed under curcumin concentrations ranging from 0.1 to 0.4 g/L (screened by the preliminary experiment) with particle size between 269 and 287 nm, zeta potential around -38 mV, and curcumin loading capacity ranging from 3.61 to 9.14 mg/g. Curcumin primarily interacts with whey protein through hydrophobic interactions and hydrogen bonds, as confirmed by FT-IR spectroscopy and molecular docking analysis. Curcumin has a different affinity to proteins ranked as bovine serum albumin (BSA) > β-lactoglobulin (β-LG) > α-lactalbumin (α-LA). Curcumin exists in an amorphous state within the protein, which also increases the surface hydrophobicity of the protein (from 565 to 687 AU) and leads to quenching intrinsic fluorescence of the protein. The binding of curcumin causes a transition from random coil to β-sheet in the protein's secondary structure but has a limited impact on its tertiary structure. Stability analysis shows that the complex remains stable in environments with 100-500 mM NaCl and heat treatment at 60-90 °C. digestion results indicate that the complex aggregates during simulated gastric fluid digestion and decompose during simulated intestinal fluid digestion, effectively enhancing the bioaccessibility of free curcumin by 60 % ( < 0.05). This study provides a theoretical basis for the green processing of protein-based oral delivery systems for lipophilic compounds.
本研究探讨了以乳清蛋白为壁材，采用简单且环保（不使用有机溶剂）的pH诱导蛋白质-多酚共组装策略开发姜黄素肠道递送系统的可行性。结果表明，在姜黄素浓度为0.1至0.4 g/L（通过初步实验筛选）的条件下形成了稳定的复合物，粒径在269至287 nm之间，ζ电位约为-38 mV，姜黄素负载量在3.61至9.14 mg/g之间。傅里叶变换红外光谱（FT-IR）和分子对接分析证实，姜黄素主要通过疏水相互作用和氢键与乳清蛋白相互作用。姜黄素对蛋白质的亲和力不同，顺序为牛血清白蛋白（BSA）>β-乳球蛋白（β-LG）>α-乳白蛋白（α-LA）。姜黄素以无定形状态存在于蛋白质中，这也增加了蛋白质的表面疏水性（从565至687 AU）并导致蛋白质的固有荧光猝灭。姜黄素的结合导致蛋白质二级结构从无规卷曲转变为β-折叠，但对其三级结构影响有限。稳定性分析表明，该复合物在含有100 - 500 mM NaCl的环境中以及在60 - 90°C热处理下保持稳定。消化结果表明，该复合物在模拟胃液消化过程中聚集，在模拟肠液消化过程中分解，有效地将游离姜黄素的生物可及性提高了60%（P<0.05）。本研究为亲脂性化合物基于蛋白质的口服递送系统的绿色加工提供了理论依据。
