Preparation and identification of angiotensin I-converting enzyme inhibitory peptides from sweet potato protein by enzymatic hydrolysis under high hydrostatic pressure

文献类型： 外文期刊

第一作者： Nazir, Muhammad Amer

作者： Nazir, Muhammad Amer;Mu, Tai-Hua;Zhang, Miao;Nazir, Muhammad Amer;Mu, Tai-Hua;Zhang, Miao

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关键词： ACE inhibitory peptides; enzymatic hydrolysis; high hydrostatic pressure; LC-MS; MS; sweet potato protein hydrolysates

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： 0950-5423

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收录情况： SCI

摘要： Sweet potato protein hydrolysates (SPPH) with angiotensin I-converting enzyme (ACE) inhibitory activity were prepared by papain, pepsin and alcalase under high hydrostatic pressure (HHP, 100-300 MPa). HHP significantly increased degree of hydrolysis (DH), nitrogen recovery (NR) and molecular weight (MW) <3 kDa fractions contents of SPPH by all three enzymes (P < 0.05). MW < 3 kDa peptide fractions from SPPH by alcalase under 100 MPa showed the highest ACE inhibitory activity (IC50 value 32.24 mu g mL(-1)), and was subjected to purification and identification by semi-preparative RP-HPLC and LC-MS/MS. Fifty-four peptides ranged from 501.28 to 1958.88 Da with 5-18 amino acids were identified and matched sporamin A and B sequences. Five identified peptides with sequences of VSAIW, AIWGA, FVIKP, VVMPSTF and FHDPMLR displayed good ACE inhibitory activity with the contribution of Val, Trp, Phe and Arg. Thus, SPPH by enzymatic hydrolysis under HHP can be potentially used in functional food.

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