食品科学 ›› 2026, Vol. 47 ›› Issue (10): 55-62.doi: 10.7506/spkx1002-6630-20250921-160

• 基础研究 • 上一篇    下一篇

海藻酸钠对黄嘌呤氧化酶活性的抑制作用及其抑制机制

杨蕊羽,李鹤宾,朱远翔,洪涛,郑明静,姜泽东,倪辉,朱艳冰   

  1. (1.集美大学海洋食品与生物工程学院,福建 厦门 361021;2.厦门医学院药学院,福建 厦门 361023;3.福建省食品微生物与酶工程重点实验室,福建 厦门 361021)
  • 出版日期:2026-05-25 发布日期:2026-06-10
  • 基金资助:
    国家自然科学基金面上项目(22178142);福建省科技计划高校产学合作项目(2024Y4008)

Inhibitory Effect and Mechanism of Sodium Alginate on the Activity of Xanthine Oxidase

YANG Ruiyu, LI Hebin, ZHU Yuanxiang, HONG Tao, ZHENG Mingjing, JIANG Zedong, NI Hui, ZHU Yanbing   

  1. (1. College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China; 2. School of Pharmacy, Xiamen Medical College, Xiamen 361023, China; 3. Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China)
  • Online:2026-05-25 Published:2026-06-10

摘要: 为探究褐藻胶对黄嘌呤氧化酶(xanthine oxidase,XO)的抑制作用及其机制,并评估其作为缓解高尿酸血症的天然抑制剂或功能性食品补充剂的潜力,本研究以海藻酸钠(sodium alginate,SA)为模型化合物,综合运用酶促动力学、荧光光谱、时间分辨荧光光谱和圆二色光谱等技术进行分析。酶促动力学结果表明,SA对XO活性呈现可逆的混合型抑制,SA质量浓度为10 mg/mL时,抑制率达到45.42%。荧光光谱分析显示,SA通过静态猝灭机制降低XO的内源荧光强度,两者在单一结合位点发生相互作用。时间分辨荧光分析结果进一步证实了SA对XO固有荧光猝灭属于静态猝灭过程。圆二色光谱分析表明,SA诱导了XO二级结构的改变和构象的变化。综上,SA可通过与XO活性位点结合并诱导酶蛋白构象变化,有效抑制其活性,本研究可为开发相关功能性食品或治疗剂奠定理论基础。

关键词: 海藻酸钠;黄嘌呤氧化酶;抑制作用;作用机制

Abstract: This study aimed to investigate the inhibitory effect and mechanism of alginate on xanthine oxidase (XO), and to evaluate its potential as a natural inhibitor or functional food supplement for alleviating hyperuricemia. Sodium alginate (SA) was used as a model compound. Enzymatic kinetics, fluorescence spectroscopy, time-resolved fluorescence spectroscopy (TRFS) and circular dichroism (CD) spectroscopy were employed for comprehensive analysis. The enzymatic kinetics results indicated that SA inhibited XO activity in a reversible mixed-type manner with an inhibition rate of 45.42% at a concentration of 10 mg/mL. Fluorescence spectroscopy analysis revealed that SA reduced the intrinsic fluorescence intensity of XO through a static quenching mechanism, with the interaction occurring at a single binding site. TRFS analysis further confirmed the static quenching process. CD spectroscopy demonstrated that SA induced secondary structural and conformational alterations in XO. The findings suggest that SA effectively inhibits XO activity by binding to its active site and inducing conformational changes in the enzyme, providing a theoretical foundation for the development of related functional foods or therapeutic agents.

Key words: sodium alginate; xanthine oxidase; inhibition; mechanism of action

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