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

Summary 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...

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Bibliographic Details
Published inInternational journal of food science & technology Vol. 55; no. 2; pp. 482 - 489
Main Authors Nazir, Muhammad Amer, Mu, Tai‐Hua, Zhang, Miao
Format Journal Article
LanguageEnglish
Published Oxford Wiley Subscription Services, Inc 01.02.2020
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Summary:Summary 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 µg 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. Angiotensin I‐converting enzyme (ACE) inhibitory peptides from sweet potato protein (SPP) by enzymatic hydrolysis with Papain, Pepsin and Alcalalse under high hydrostatic pressure (HHP) were prepared and identified.
ISSN:0950-5423
1365-2621
DOI:10.1111/ijfs.14291