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鹿茸冻干粉的酶解及其酶解产物性质的研究 被引量:3

Enzymatic hydrolysis of antler and properties of hydrolysates
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摘要 目的:通过研究鹿茸冻干粉酶解产物的促成骨细胞增殖活性,抗氧化性以及血管紧张素转化酶I(angiotensin Iconverting enzyme,ACE,EC3.4.15.1)抑制活性,为阐明鹿茸强筋健骨的机制以及揭示鹿茸体内生理功能发挥的机制提供研究线索。方法:采用体内常见的消化酶胃蛋白酶和胰蛋白酶分别和同时对鹿茸冻干粉进行酶解,确定酶解完全的条件,收集相对分子质量小于1万的多肽混合物,对其抗氧化性,ACE抑制活性以及促成骨细胞增殖活性进行研究。结果:鹿茸冻干粉的不同酶解产物对羟自由基的清除效果非常明显,其IC50均低1g·L-1,远低于维生素C的5.5g·L-1,同时胃蛋白酶和双酶酶解产物对ACE抑制效果极佳,胰蛋白酶酶解产物对大鼠成骨细胞(UMR-106细胞)的促增殖作用达73.43%。结论:本实验进一步验证了鹿茸强筋健骨以及强身抗老等传统功效,对于ACE抑制活性的试探性研究也表明鹿茸酶解产物具有潜在的高血压防治功能;本实验结果也为进一步分离提取鹿茸酶解产物中的抗氧化性多肽,ACE抑制活性肽以及促成骨细胞活性肽提供强有力的依据。 Lyophylized antler powder was hydrolyzed by pepsin and trypsin separately and also simultaneously to give hydrolysates with special physical activities. Complete hydrolysis peptides with MW lower than 1×103 were collected for assay of angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant activity and proliferative activity toward UMR-106 osteoblast cells. The results of the experiments revealed that all hydrolysates exhibited potent hydroxyl radical scavenging activity with an IC50 value less than 1mg/ml which was much lower than the value of 5.5 g·L-1 for vitamin C. The peptic and peptic tryptic hydrolysates demonstrated strong angiotensin I-converting enzyme (ACE) inhibitory activity. The tryptic hydrolysate increased the proliferation of the UMR-106 cells by 73.43%. The results verified the traditional use of antler in bone-strengthening, anti-aging. The exploratory studies on the ACE inhibitory activity of antler hydrolysates indicated that the hydrolysates might be potentially useful in prevention and treatment of hypertension. Further purification of peptides contributing to the antioxidant activity, angiotensin I-converting enzyme-inhibitory activity and proliferative activity toward osteoblasts from antler hydrolysates is warranted.
出处 《中国中药杂志》 CAS CSCD 北大核心 2010年第19期2628-2633,共6页 China Journal of Chinese Materia Medica
基金 国家自然科学基金项目(20672021)
关键词 鹿茸 酶解 成骨细胞 ACE抑制活性 抗氧化性 antler hydrolysis UMR-106 cell ACE inhibitory activity antioxidant activity
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