Novel antihypertensive peptides from lupin protein hydrolysate: An in-silico identification and molecular docking studies

Gbemisola J. Fadimu, Chee Yuen Gan, Olusegun A. Olalere, Asgar Farahnaky, Harsharn Gill, Tuyen Truong

Research output: Contribution to journalArticlepeer-review

4 Citations (SciVal)

Abstract

Application of non-thermal treatment to proteins prior to enzymatic hydrolysis can facilitate the release of novel bioactive peptides (BPs) with unique biological activities. In this study, lupin protein isolate was pre-treated with ultrasound and hydrolysed using alcalase and flavourzyme to produce alcalase hydrolysate (ACT) and flavourzyme hydrolysate (FCT). These hydrolysates were fractionated into 1, 5, and 10 kDa molecular weight fractions using a membrane ultrafiltration technique. The in vitro angiotensin-converting enzyme (ACE) studies revealed that unfractionated ACT (IC50 = 3.21 mg mL−1) and FCT (IC50 = 3.32 mg mL−1) were more active inhibitors of ACE in comparison to their ultrafiltrated fractions with IC50 values ranging from 6.09 to 7.45 mg mL−1. Molecular docking analysis predicted three unique peptides from ACT (AIPPGIPY, SVPGCT, and QGAGG) and FCT (AIPINNPGKL, SGNQGP, and PPGIP) as potential ACE inhibitors. Thus, unique BPs with ACE inhibitory effects might be generated from ultrasonicated lupin protein.

Original languageEnglish
Article number135082
JournalFood Chemistry
Volume407
Early online date28 Nov 2022
DOIs
Publication statusPublished - 1 May 2023

Keywords

  • ACE
  • Alcalase
  • Antihypertensive peptide
  • Bioactive peptides
  • Flavourzyme
  • Lupin protein hydrolysate

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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