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Preparation and identification of angiotensin I‐converting enzyme inhibitory peptides from sweet potato protein by enzymatic hydrolysis under high hydrostatic pressure
Author(s) -
Nazir Muhammad Amer,
Mu TaiHua,
Zhang Miao
Publication year - 2020
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14291
Subject(s) - chemistry , hydrolysate , papain , enzyme , hydrolysis , enzymatic hydrolysis , hydrostatic pressure , pepsin , chromatography , peptide , biochemistry , angiotensin converting enzyme , biology , blood pressure , physics , thermodynamics , endocrinology
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 (IC 50 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.