Purification and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from abalone (Haliotis discus hannai Ino) gonads

被引：44

作者：

Wu, Qiang ^{[1
,2
]}

Cai, Qiu-Feng ^{[1
,2
]}

Tao, Zhi-Peng ^{[1
,2
]}

Sun, Le-Chang ^{[1
,2
]}

Shen, Jian-Dong ^{[1
,2
]}

Zhang, Ling-Jing ^{[1
,2
]}

Liu, Guang-Ming ^{[1
,2
]}

Cao, Min-Jie ^{[1
,2
]}

机构：

[1] Jimei Univ, Coll Food & Biol Engn, Xiamen 361021, Peoples R China

[2] Fujian Collaborat Innovat Ctr Exploitat & Utiliza, Xiamen 361102, Fujian Province, Peoples R China

来源：

EUROPEAN FOOD RESEARCH AND TECHNOLOGY | 2015年 / 240卷 / 01期

关键词：

Abalone Haliotis Discus Hannai Ino; Gonads; ACE inhibitory peptide; Purification; Gastrointestinal digestion; PROTEIN HYDROLYSATE; LYSOZYME;

D O I：

10.1007/s00217-014-2315-8

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Abalone gonads were hydrolyzed using alcalase followed by papain to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Gel filtration column chromatography analysis showed that the molecular weight of the fraction with high ACE inhibitory activity was below 1 kDa, which occupied 93.1 % of total hydrolysate. The ACE inhibitory peptide was purified by a series of column chromatographies, and the sequence of purified peptide was further identified as Ala-Met-Asn (AMN) by automated Edman degradation method. The triple peptide was then synthesized and had an ACE inhibitory activity with IC50 value of 106.24 mu g/mL. After gastrointestinal digestion, the peptide still remained bioactivity. Lineweaver-Burk plots indicated that AMN acts as a non-competitive inhibitor against ACE. Our present study suggested that AMN derived from abalone gonad by-products may be used as an ideal nutrient for development of functional foods.

引用

页码：137 / 145

页数：9

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