State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo 315211, China.
Department of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiao Tong, Shanghai 200240, China.
Int J Mol Sci. 2023 Apr 1;24(7):6582. doi: 10.3390/ijms24076582.
Flavonoids are easily destroyed and their activity lost during gastrointestinal digestion. Protein-based nanocomplexes, a delivery system that promotes nutrient stability and bioactivity, have received increasing attention in recent years. This study investigated the stability, inhibitory activity against α-glucosidase and interaction mechanisms of protein-based nanocomplexes combining whey protein isolate (WPI), soybean protein isolate (SPI) and bovine serum albumin (BSA) with flavonoids (F) from using spectrophotometry, fluorescence spectra and molecular docking approaches. The results show that the flavonoid content of WPI-F (23.17 ± 0.86 mg/g) was higher than those of SPI-F (19.41 ± 0.56 mg/g) and BSA-F (20.15 ± 0.62 mg/g) after simulated digestion in vitro. Furthermore, the inhibition rate of WPI-F (23.63 ± 0.02%) against α-glucosidase was also better than those of SPI-F (18.56 ± 0.02%) and BSA-F (21.62 ± 0.02%). The inhibition rate of WPI-F increased to nearly double that of F alone (12.43 ± 0.02%) ( < 0.05). Molecular docking results indicated that the protein-flavonoids (P-F) binding occurs primarily through hydrophobic forces, hydrogen bonds and ionic bonds. Thermodynamic analysis (ΔH > 0, ΔS > 0) indicated that the P-F interactions are predominantly hydrophobic forces. In addition, the absolute value of ΔG for WPI-F is greater (-30.22 ± 2.69 kJ mol), indicating that WPI-F releases more heat energy when synthesized and is more conducive to combination. This paper serves as a valuable reference for the stability and bioactivity of flavonoids from .
黄酮类化合物在胃肠道消化过程中很容易被破坏，其活性也会丧失。近年来，基于蛋白质的纳米复合物作为一种促进营养物质稳定性和生物活性的递送系统，受到了越来越多的关注。本研究采用分光光度法、荧光光谱法和分子对接方法，研究了乳清蛋白分离物（WPI）、大豆蛋白分离物（SPI）和牛血清白蛋白（BSA）与 中黄酮类化合物（F）结合形成的基于蛋白质的纳米复合物的稳定性、对α-葡萄糖苷酶的抑制活性及其相互作用机制。结果表明，体外模拟消化后，WPI-F（23.17±0.86mg/g）中的黄酮类化合物含量高于 SPI-F（19.41±0.56mg/g）和 BSA-F（20.15±0.62mg/g）。此外，WPI-F（23.63±0.02%）对α-葡萄糖苷酶的抑制率也优于 SPI-F（18.56±0.02%）和 BSA-F（21.62±0.02%）。WPI-F 的抑制率增加到几乎是 F 单独作用的两倍（12.43±0.02%）（<0.05）。分子对接结果表明，蛋白质-黄酮（P-F）结合主要通过疏水作用力、氢键和离子键发生。热力学分析（ΔH>0，ΔS>0）表明，P-F 相互作用主要是疏水作用力。此外，WPI-F 的ΔG 的绝对值较大（-30.22±2.69kJ/mol），表明 WPI-F 在合成时释放出更多的热能，更有利于结合。本文为 中黄酮类化合物的稳定性和生物活性提供了有价值的参考。
