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Interaction of Bovine Serum Albumin with Naringenin and Its Effect on the Stability of Naringenin
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Kaixin SHI1, Li LI1, Yan GUO1, *, Yilin GUO1, Jinchang TONG1, Boping LIU2, 3, *, Jianguo XU1, *
Science and Technology of Food Industry | 2026, 47(10) : 107 - 119
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Science and Technology of Food Industry | 2026, 47(10): 107-119
• Research and Investigation •
Interaction of Bovine Serum Albumin with Naringenin and Its Effect on the Stability of Naringenin
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Kaixin SHI1, Li LI1, Yan GUO1, *, Yilin GUO1, Jinchang TONG1, Boping LIU2, 3, *, Jianguo XU1, *
Affiliations
  • 1College of Food Science, Shanxi Normal University, Taiyuan 030031, China
  • 2College of Materials and Energy, South China Agricultural University, Guangzhou 510630, China
  • 3Key Laboratory for Bio-based Materials and Energy of Ministry of Education,South China Agricultural University, Guangzhou 510630, China
Published: 2026-05-15 doi: 10.13386/j.issn1002-0306.2025050226
Outline
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To investigate the interaction mechanism between bovine serum albumin (BSA) and naringenin (Nar), as well as the impact on the stability of Nar, multi-spectroscopic techniques were initially utilized to study the quenching mechanism, binding constant, and binding site of the BSA-Nar complex. Subsequently, molecular dynamics simulations were conducted to explore the binding free energy, key residues, binding modes, and interactions. Finally, Nar/BSA nanoparticles (Nar/BSA NPs) were prepared, and the antioxidant activity and in vitro release properties were examined. The findings indicated that Nar could quench the intrinsic fluorescence of BSA through a static quenching mechanism. The BSA-Nar complex was primarily formed via hydrogen bonding and hydrophobic interactions, with a binding constant of 1.7×104 L/mol and a binding free energy of -14.78 kcal/mol. The secondary structure of BSA was altered, with the α-helix content decreasing from 79.39% to 77.67%. There was approximately one binding site between BSA and Nar, and Nar binds to site I of BSA. Key residues Arg208, Ala212, Leu326, and Gly327 significantly contributed to the binding. Furthermore, after six days of storage, when the concentration was 40 µg/mL, the DPPH free radical scavenging rates of Nar/BSA NPs and Nar were 11.42% and 9.30%, respectively. Following 61 hours of simulated gastric fluid digestion, the release rates of Nar/BSA NPs and Nar were 62% and 79%, respectively. The corresponding release rates in simulated intestinal fluids were 86% and 89%, respectively. These results demonstrate that BSA can stably bind with Nar, and the antioxidant activity of Nar is significantly enhanced upon encapsulation with BSA. Additionally, the release rates of Nar in simulated gastric and intestinal fluids are slowed when encapsulated within BSA.

naringenin (Nar)  /  bovine serum albumin (BSA)  /  spectroscopy  /  molecular dynamics simulation  /  interaction mechanism
施凯欣, 李丽, 郭妍, 郭怡琳, 仝晋昌, 刘柏平, 徐建国. 牛血清白蛋白与柚皮素相互作用及对柚皮素稳定性的影响. 食品工业科技, 2026 , 47 (10) : 107 -119 . DOI: 10.13386/j.issn1002-0306.2025050226
Kaixin SHI, Li LI, Yan GUO, Yilin GUO, Jinchang TONG, Boping LIU, Jianguo XU. Interaction of Bovine Serum Albumin with Naringenin and Its Effect on the Stability of Naringenin[J]. Science and Technology of Food Industry, 2026 , 47 (10) : 107 -119 . DOI: 10.13386/j.issn1002-0306.2025050226
Year 2026 volume 47 Issue 10
157
67
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Article Info
doi: 10.13386/j.issn1002-0306.2025050226
  • Receive Date:2025-05-26
  • Online Date:2026-10-24
  • Published:2026-05-15
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  • Received:2025-05-26
Affiliations
    1College of Food Science, Shanxi Normal University, Taiyuan 030031, China
    2College of Materials and Energy, South China Agricultural University, Guangzhou 510630, China
    3Key Laboratory for Bio-based Materials and Energy of Ministry of Education,South China Agricultural University, Guangzhou 510630, China
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表12种不同金属材料的力学参数
科
Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)
属
Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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