TY - JOUR
T1 - Novel antihypertensive peptides from lupin protein hydrolysate: An in-silico identification and molecular docking studies
AU - Fadimu, Gbemisola J.
AU - Gan, Chee Yuen
AU - Olalere, Olusegun A.
AU - Farahnaky, Asgar
AU - Gill, Harsharn
AU - Truong, Tuyen
N1 - Funding Information:
The first author acknowledges the support from Royal Melbourne Institute of Technology (RMIT University) for his PhD program.
PY - 2022/11/28
Y1 - 2022/11/28
N2 - 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.
AB - 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.
KW - ACE
KW - Alcalase
KW - Antihypertensive peptide
KW - Bioactive peptides
KW - Flavourzyme
KW - Lupin protein hydrolysate
UR - http://www.scopus.com/inward/record.url?scp=85144024976&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2022.135082
DO - 10.1016/j.foodchem.2022.135082
M3 - Article
C2 - 36493485
AN - SCOPUS:85144024976
VL - 407
JO - Food Chemistry
JF - Food Chemistry
SN - 0308-8146
M1 - 135082
ER -