食品科学 ›› 2026, Vol. 47 ›› Issue (14): 126-135.doi: 10.7506/spkx1002-6630-20260108-067

• 食品化学 • 上一篇    

蓝莓花青素/蚕豆蛋白复合物的相互作用机制及其理化性质与体外模拟消化分析

王冰,李松林,张丽霞   

  1. (1.江苏省农业科学院农产品加工研究所,江苏?南京 210014;2.淮阴工学院生命科学与食品工程学院,江苏?淮安 223001)
  • 发布日期:2026-08-24
  • 基金资助:
    江苏省政府留学基金项目(29011904);山东省科技型中小企业创新能力提升工程项目(2023TSGC0489)

Interaction Mechanism, Physicochemical Properties, and in Vitro Simulated Digestion Characteristics of Blueberry Anthocyanin/Fava Bean Protein Complexes

WANG Bing, LI Songlin, ZHANG Lixia   

  1. (1. Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China; 2. School of Life Sciences and Food Engineering, Huaiyin Institute of Technology, Huai’an 223001, China)
  • Published:2026-08-24

摘要: 探究不同添加量的蓝莓花青素(blueberry anthocyanin,BA)与蚕豆蛋白(Vicia faba protein,VFP)复合物的理化特性及功能性质。通过构建低、中、高3 种花青素添加量的复合物(L-BA、M-BA、H-BA),采用粒径分布对复合物进行表征,运用紫外-可见吸收光谱、荧光光谱、分子对接等技术手段,探究花青素添加量对BA-VFP复合物相互作用的影响机制。在此基础上,研究复合物的色泽、持水性与持油性、起泡性与泡沫稳定性、乳化性与乳化稳定性以及体外模拟消化特性。结果表明,随着花青素添加量的增加,复合物粒径降低且分布更为集中。紫外-可见吸收光谱显示复合物特征吸收峰发生红移,同时蛋白质内源荧光强度呈浓度依赖性降低(P<0.05)。同步荧光光谱进一步表明,色氨酸和酪氨酸残基的微环境疏水性随花青素添加量增加而显著增强(P<0.05)。分子对接模拟揭示,花青素通过氢键、疏水相互作用和π-阳离子作用与蛋白质活性位点结合。花青素添加量与pH值协同决定了复合物的颜色变化。适量花青素添加显著提升复合物的持水性与持油性(P<0.05),但过量添加会导致起泡性、乳化性及相关稳定性降低。体外模拟消化实验表明,复合物可有效维持花青素的消化稳定性,其中H-BA的花青素保留率达74.34%,2,2′-联氮双(3-乙基苯并噻唑啉-6-磺酸)阳离子自由基清除率、1,1-二苯基-2-三硝基苯肼自由基清除率及铁离子还原力均显著高于BA(P<0.05),表明复合物形成有效维持花青素稳定性及其抗氧化活性。本研究为BA-VFP复合物在功能性食品中的应用提供了理论依据。

关键词: 蓝莓花青素;蚕豆蛋白;复合物;相互作用;理化特性;体外消化

Abstract: This study investigated the effects of different addition levels (high, middle, low) of blueberry anthocyanins (BA) on the interactions, physicochemical properties, and in vitro simulated digestion characteristics of complexes formed between BA and Vicia faba protein (VFP), designated as L-BA, M-BA, and H-BA. Particle size distribution was used to characterize the complexes. The mechanism underlying the influence of BA concentration on its interaction with VFP was explored using ultraviolet-visible (UV-Vis) absorption spectroscopy, fluorescence spectroscopy, and molecular docking. Furthermore, the color, water-holding capacity (WHC), oil-holding capacity (OHC), foaming properties, emulsifying properties, and in vitro simulated digestion characteristics of the complexes were studied. The results showed that as BA concentration increased, the particle size of the complexes decreased and the particle size distribution became more uniform. UV-Vis absorption spectra indicated a red-shift in the characteristic absorption peaks of the complexes. Additionally, the intrinsic fluorescence intensity of the protein decreased in a concentration-dependent manner (P < 0.05). Synchronous fluorescence spectroscopy further revealed that the hydrophobicity of the microenvironment around tryptophan and tyrosine residues increased significantly with increasing concentration of BA (P < 0.05). Molecular docking simulations suggested that anthocyanins bound to the protein’s active sites through hydrogen bonding, hydrophobic interactions, and π-cation interactions. BA concentration and pH cooperatively determined the color changes of the complexes. Moderate BA addition significantly enhanced the WHC and OHC of the complexes (P < 0.05), while excessive addition led to a reduction in the foaming capacity, foam stability, emulsifying capacity, and emulsion stability. In vitro simulated digestion experiments demonstrated that the complexes effectively maintained the digestive stability of anthocyanins. Specifically, the H-BA complex achieved a BA retention rate of 74.34%. Furthermore, the 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) cation radical scavenging activity, 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, and ferric reducing power of the complexes were significantly higher than those of free BA (P < 0.05). Collectively, complexation with VFP effectively preserved BA stability and its antioxidant activity. This study provides a theoretical foundation for the application of BA-VFP complexes in functional foods.

Key words: blueberry anthocyanins; Vicia faba protein; complexes; interaction; physicochemical properties; in vitro digestion

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