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• W4229057310 endingPage "1355" @default.
• W4229057310 startingPage "1355" @default.
• W4229057310 abstract "The addition of food-derived antihypertensive peptides to the diet is considered a reasonable antihypertension strategy. However, data about the stability of antihypertensive peptides in different food processing conditions are limited. In this study, through Sephadex G-15 gel chromatography and RP-HPLC separation, UPLC-ESI-MS/MS analysis and in silico screening, two novel ACE-inhibitory peptides, Pro-Leu-Leu-Lys (IC50: 549.87 μmol/L) and Pro-Pro-Met-Trp-Pro-Phe-Val (IC50: 364.62 μmol/L), were identified in millet bran glutelin-2 hydrolysates. The inhibition of angiotensin-I converting enzyme and the potential safety of PLLK and PPMWPFV were studied using molecular docking and in silico prediction, respectively. The results demonstrated that PLLK and PPMWPFV could non-competitively bind to one and seven binding sites of ACE through short hydrogen bonds, respectively. Both PLLK and PPMWPFV were resistant to different pH values (2.0-10.0), pasteurization conditions, addition of Na+, Mg2+ or K+ and simulated gastrointestinal digestion. However, PLLK and PPMWPFV were unstable upon heat treatment at 100 °C for more than 20 min or treatment with Fe3+ or Zn2+. In fact, treatment with Fe3+ or Zn2+ induced the formation of PLLK-iron or PLLK-zinc chelates and reduced the ACE-inhibitory activity of PLLK. These results indicate that peptides derived from millet bran could be added to foods as antihypertension agents." @default.
• W4229057310 created "2022-05-08" @default.
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• W4229057310 date "2022-05-06" @default.
• W4229057310 modified "2023-09-29" @default.
• W4229057310 title "Two Novel Antihypertensive Peptides Identified in Millet Bran Glutelin-2 Hydrolysates: Purification, In Silico Characterization, Molecular Docking with ACE and Stability in Various Food Processing Conditions" @default.
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• W4229057310 doi "https://doi.org/10.3390/foods11091355" @default.
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• W4229057310 hasPublicationYear "2022" @default.
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