Grass carp peptides hydrolysed by the combination of Alcalase and Neutrase: Angiotensin-I converting enzyme (ACE) inhibitory activity, antioxidant activities and physicochemical profiles

文献类型： 外文期刊

第一作者： Chen, Jiwang

作者： Chen, Jiwang;Chen, Yue;Xia, Wenshui;Xiong, Youling L.;Wang, Hongxun;Chen, Jiwang;Xiong, Youling L.;Wang, Hongxun;Xia, Wenshui;Ye, Ran

作者机构：

关键词： angiotensin-I converting enzyme (ACE) inhibitory activity;antioxidant activities;enzymatic hydrolysis;grass carp peptides

期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：3.713； 五年影响因子：3.408 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： In this study, grass carp peptides were prepared by enzymatic hydrolysis of grass carp protein using the combination of Alcalase and Neutrase, and angiotensin-I converting enzyme (ACE) inhibitory activity in vitro, antihypertensive activity in vivo, antioxidant activities, and physicochemical properties of peptides achieved from grass carp protein were characterised after ultrafiltration and desalted processes using mixed ion exchange resins. The purified peptides exhibited strong ACE inhibitory activity (IC50 = 105 lg mL(-1)), antihypertensive activity with the maximal drop for systolic blood pressure (SBP) of 43 mmHg at a dosage of 100 mg per kg body weight in spontaneously hypertensive rat (SHR), and antioxidant activities indicated by thiobarbituric acid-reactive substance values in a liposome-oxidising system, radical-scavenging activity and chelation of metal ions (Fe2+). The molecular weight of peptides was <1000 Da. Compared to grass carp protein, the peptides separated from enzymatic hydrolysates possessed similar amino acid compositions, but contained higher concentrations of essential amino acids. Moreover, the peptides exhibited excellent solubility at a wide range of pH values from 2 to 10, and lower apparent viscosity than the protein. The peptides separated from enzymatic hydrolysates might be used as a promising ingredient in antihypertensive functional foods and nutraceuticals.

分类号： TS2

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