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• W2960871877 abstract "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." @default.
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• W2960871877 date "2019-08-11" @default.
• W2960871877 modified "2023-09-27" @default.
• W2960871877 title "Preparation and identification of angiotensin I‐converting enzyme inhibitory peptides from sweet potato protein by enzymatic hydrolysis under high hydrostatic pressure" @default.
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• W2960871877 doi "https://doi.org/10.1111/ijfs.14291" @default.
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