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海地瓜蛋白水解物中ACE抑制肽的分离纯化及合成
Purification and synthesis of ACE inhibitory peptide from Acaudina molpadioidea protein hydrolysate
【作者】 赵元晖; 李八方; 董士远; 刘尊英; 赵雪; 王静凤; 曾名湧;
【Author】 ZHAO Yuan-hui,LI Ba-fang,DONG Shi-yuan,LIU Zun-ying,ZHAO Xue,WANG Jing-feng,ZENG Ming-yong (Lab of Aquatic Products Utilization,College of Food Science and Engineering,Ocean University of China,Qingdao 266003, China)
【机构】 中国海洋大学食品科学与工程学院水产品高值化利用实验室;
【摘要】 利用Sephadex G-25凝胶柱层析、SP Sephadex C-25阳离子交换层析、反相高效液相色谱层析对海地瓜水解产物进行分离纯化,得到高活性的ACE抑制肽,其氨基酸序列为MEGAQEAQGD,IC50值为15.9μM。采用逐步缩合和片断缩合相结合的方法对海地瓜ACE抑制肽MEGAQEAQGD进行了设计合成。该合成肽的纯度为99.72%,分子量与序列结构均与理论值相符。研究发现抑制肽与胃肠蛋白酶水解反应后,活性增强了3.5倍。动物实验表明,剂量为3μM/kg的抑制肽对自发性高压大鼠具有明显的降压效果。
【Abstract】 An ACE inhibitory peptide was isolated from the sea cucumber(Acaudina molpadioidea) hydrolysate,using the chromatographic methods including gel filtration,ion-exchange chromatography and reversed phase high-performance liquid chromatography.The purified ACE inhibitory peptide was sequenced as MEGAQEAQGD,with IC50 value of 15.9 uM.The ACE inhibitory peptide was synthesized by a method of gradual condensation and fragmental condensation.The purity of the decapeptide was 99.72%,and the molecular weight and sequence structure of the decapeptide equate with the fact.It was found that the inhibitory activity of the peptide was intensified by 3.5 times after incubation with gastrointestinal proteases.The ACE inhibitory peptide from Acaudina molpadioidea showed a clear antihypertensive effect in spontaneously hypertensive rats(SHR),at a dosage of 3μM/kg.
【Key words】 Acaudina molpadioidea; ACE inhibitory peptide; isolation and purification; synthesis;
- 【会议录名称】 2010年中国水产学会学术年会论文摘要集
- 【会议名称】2010年中国水产学会学术年会
- 【会议时间】2010-10-21
- 【会议地点】中国陕西西安
- 【分类号】S917.4
- 【主办单位】中国水产学会