Purification of a Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptide with an Antihypertensive Effect from Loach (Misgurnus anguillicaudatus)

被引：52
作者：
Li, Ying [1 ,2 ]
Zhou, Jianzhong [2 ]
Huang, Kaihong [2 ]
Sun, Yi [1 ]
Zeng, Xiaoxiong [1 ]
机构：
[1] Nanjing Agr Univ, Coll Food Sci & Technol, Nanjing 210095, Jiangsu, Peoples R China
[2] Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Jiangsu, Peoples R China
来源：
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2012年 / 60卷 / 05期
关键词：
loach (Misgurnus anguillicaudatus); ACE inhibitory peptide; mass spectrometry; antihypertensive effect; FRAME PROTEIN; BY-PRODUCTS; IDENTIFICATION; HYDROLYSATE;
D O I：
10.1021/jf204118n
中图分类号：
S [农业科学];
学科分类号：
09 ;
摘要：
To isolate and characterize novel angiotensin I-converting enzyme (ACE) inhibitory peptide from loach (Misgurnus anguillicaudatus), six proteases, pepsin, alpha-chymotrypsin, bromelain, papain, alcalase, and Neutrase, were used to hydrolyze loath protein. The hydrolysate (LPH) generated by bromelain [ratio of enzyme to substrate, 3:1000 (w/w)] was found to have the highest ACE inhibitory activity (IC50, 613.2 +/- 8.3 mu g/mL). Therefore, it was treated by ultrafiltration to afford fraction of LPH-IV (MW < 2.5 kDa) with an IC50 of 231.2 +/- 3.8 mu g/mL, having higher activity than the other fractions. Then, LPH-IV was isolated and purified by consecutive purification steps of gel filtration chromatography and reverse-phase high-performance liquid chromatography to afford a purified peptide with an IC50 of 18.2 +/- 0.9 mu g/mL, an increase of 33.7-fold in ACE inhibitory activity as compared with that of LPH. The purified peptide was identified as Ala-His-Leu-Leu (452 Da) by Q-TOF mass spectrometry and amino acid analyzer. An antihypertensive effect in spontaneously hypertensive rats revealed that oral administration of LPH-IV could decrease systolic blood pressure significantly.
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收藏
页码：1320 / 1325
页数：6
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