食品科学 ›› 2025, Vol. 46 ›› Issue (8): 143-150.doi: 10.7506/spkx1002-6630-20240918-137

• 营养卫生 • 上一篇    下一篇

羊骨生物活性肽体内外降尿酸活性及作用机制

李晓彤,胡冠华,王诗琪,刘培清,王生富,王富荣,乌兰花,孙立娜,靳烨,赵丽华   

  1. (1.内蒙古农业大学食品科学与工程学院,内蒙古?呼和浩特 010018;2.阿拉善左旗市场监督管理局,内蒙古?阿拉善盟 750306;3.乌兰察布市市场监督管理局,内蒙古?乌兰察布 012000;4.内蒙古自治区乡村振兴促进中心,内蒙古?呼和浩特 010018;5.包头东宝生物技术股份有限公司,内蒙古?包头 014000;6.乌拉特中旗农牧和科技局,内蒙古?巴彦淖尔 015000)
  • 出版日期:2025-04-25 发布日期:2025-04-09
  • 基金资助:
    中央引导地方科技发展资金项目(2024ZY0097);内蒙古自治区科技计划项目(2023YFSH0058); “科技兴蒙”行动重点专项(NMKJXM202210)

Uric Acid-Lowering Activity in Vitro and in Vivo and Mechanism of Sheep Bone Bioactive Peptides

LI Xiaotong, HU Guanhua, WANG Shiqi, LIU Peiqing, WANG Shengfu, WANG Furong, WULAN Hua, SUN Lina, JIN Ye, ZHAO Lihua   

  1. (1. College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot 010018, China; 2. Alxa Left Banner Market Supervision and Administration Bureau, Alxa League 750306, China; 3. Ulanqab Municipal Market Supervision Administration, Ulanqab 012000, China; 4. Inner Mongolia Autonomous Region Rural Revitalization Promotion Center, Hohhot 010018, China; 5. Baotou Dongbao Biotechnology Co. Ltd., Baotou 014000, China; 6. Wulatezhongqi Agriculture and Animal Husbandry and Science and Technology Bureau, Bayannaoer 015000, China)
  • Online:2025-04-25 Published:2025-04-09

摘要: 采用碱性蛋白酶和中性蛋白酶双酶分步水解法从羊骨中提取羊骨生物活性肽(sheep bone bioactive peptides,SBBP),本研究评估了其结构、氨基酸组成、分子质量分布及黄嘌呤氧化酶抑制活性。结果表明,双酶分步水解改变了羊骨蛋白的二级结构,所制备的SBBP富含疏水性氨基酸、芳香族氨基酸和碱性氨基酸,且<1 000 Da的肽段占比高达94.48%。SBBP在体外显示出黄嘌呤氧化酶抑制作用(半抑制浓度为14.27 mg/mL)。在高尿酸血症小鼠模型中,SBBP通过抑制黄嘌呤氧化酶和腺苷脱氨酶活性,显著降低血清尿酸、肌酐和尿素氮水平,并减轻肾脏组织病理学损伤。研究表明,SBBP具备预防和缓解高尿酸血症的潜力。

关键词: 黄嘌呤氧化酶;高尿酸血症;羊骨生物活性肽

Abstract: Sheep bone bioactive peptides (SBBP) were prepared by successive enzymatic hydrolysis of sheep bones by alkaline and neutral proteases. This study evaluated the structure, amino acid composition, molecular mass distribution, and xanthine oxidase inhibitory activity of SBBP. The results showed that successive enzymatic hydrolysis altered the secondary structure of sheep bone proteins. SBBP were rich in hydrophobic, aromatic, and basic amino acids. Peptides with a molecular mass less than 1 000 Da accounted for 94.48% of SBBP. SBBP exhibited xanthine oxidase inhibitory activity in vitro, with a half maximal inhibitory concentration (IC50) of 14.27 mg/mL. In a hyperuricemic mouse model, SBBP significantly reduced serum uric acid, creatinine and urea nitrogen levels by inhibiting the activity of xanthine oxidase and adenosine deaminase, and alleviated kidney damage. This study indicates that SBBP holds the potential for preventing and alleviating hyperuricemia.

Key words: xanthine oxidase; hyperuricemia; sheep bone bioactive peptides

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