摘要
实验建立一种从蛋白水解物中快速高效鉴别血管紧张素转化酶抑制剂(ACEI)的方法:先对蛋白按照酶解位点进行序列搜寻,建立一个样品肽库;在量效结构关系(QSAR)研究的基础上对样品库中的肽的ACE抑制活性进行预测,然后化学合成目标肽及测定活性;必要时用现代分析技术确证蛋白水解物中目标肽的存在。用此方法对油菜、大米、小麦蛋白水解物中三肽ACE抑制活性进行研究,发现IC50在10μmol/L以下的三肽多达34条,选择了11条活性较高的肽合成验证,最后发现潜藏在油菜Cruciferin BNC1(P33523)蛋白序列347～349的LRL活性最高,IC50达到3.42μmol/L,且具有较好的稳定性。抑制动力学研究表明,LRL属于竞争性抑制剂;油菜蛋白胃蛋白酶水解物进行分子质量分段,取分子质量小于1000D部分进行高效液相色谱(HPLC)分析发现有LRL。
A rapid and highly efficient method for identifying angiotensin I converting enzyme inhibitory peptides from protein hydrolysates was established based on quantitative structure activity relationship（QSAR） and protein sequence.First,a small peptide library was constructed by protein sequence searching according to the hydrolysis sites of a specific enzyme.Then,the activities of peptides in the library were predicted using QSAR model.Target peptides were synthesized and their IC50 values were measured.Finally,a real protein hydrolysate was prepared and HPLC was employed to analyze the target peptides in the hydrolysates.Totally 34 tripeptides with an IC50 of less than 10 μmol/L were predicted from rapeseed protein,wheat protein and rice protein and 11of them with higher activity were synthesized.LRL with the lowest IC50 of 3.42μmol/L located in rapeseed cruciferin BNC1（P33523） sequence 347—349 was characterized from the synthesized peptides.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2011年第19期120-124,共5页
Food Science
基金
重庆自然科学基金项目(2007BB0345)
关键词
血管紧张素转换酶抑制剂
QSAR
活性预测
油菜籽蛋白
大米蛋白
小麦蛋白
ACE inhibitor
quantitative structre activity relationship（QSAR）
activity prediction
rapeseed protein
wheat protein
rice protein
