Proteomic profiling of Monascus-fermented djulis (Chenopodium formosanum) identifies ACE-inhibitory peptides through integrated in silico and in vitro approaches
Journal
Food Chemistry
Journal Volume
500
ISSN
0308-8146
Date Issued
2026-01
Author(s)
Lu, Jheng-Jhe
Khumsupan, Darin
Hsieh, Chen-Che
Hsieh, Chang-Wei
Santoso, Shella Permatasari
Angkawijaya, Artik Elisa
Kuo, Hsing-Chun
Abstract
This study identified angiotensin-converting enzyme (ACE) inhibitory peptides generated during Monascus purpureus fermentation of djulis ( Chenopodium formosanum ). Protein hydrolysates from fermented dehulled djulis showed the highest ACE inhibition, reaching 40.71 ± 2 . 95 % on day 8 (captopril: 43.33 ± 3.53 %). In silico screening (BIOPEP database) and proteomics highlighted DAAGYVADK (DK9) as a potential candidate. Molecular docking indicated a binding affinity of −9.174 kcal/mol (captopril: −5.77). The binding was mainly stabilized by 7 hydrogen bonds with ACE active site residues Glu384, His353, Lys511, Gln281, Asn277, Ala354, and Arg522. Moreover, enzyme-kinetic analysis indicated competitive inhibition by increased K m with unchanged V max. Furthermore, absorption, distribution, metabolism, excretion, and toxicity (ADMET) predictions suggested low toxicity and favorable pharmacokinetic properties for DK9. These findings support Monascus -fermented dehulled djulis as a promising substrate to generate natural ACE-inhibitory peptides and identify DK9 as a lead peptide for further development.
Subjects
Angiotensin converting enzyme inhibitor
Djulis
Fermentation
Molecular docking
bioactive peptide
Monascus pupureus
Publisher
Elsevier Ltd
Description
Article number 147474
Type
journal article