TY - JOUR
T1 - A comparative analysis of anti-lipidemic potential of soybean (Glycine max) protein hydrolysates obtained from different ripening stages
T2 - Identification, and molecular interaction mechanisms of novel bioactive peptides
AU - Alnuaimi, Amna
AU - Fisayo Ajayi, Feyisola
AU - Hamdi, Marwa
AU - Mudgil, Priti
AU - Kamal, Hina
AU - Yuen Gan, Chee
AU - Maqsood, Sajid
N1 - Funding Information:
Authors would like to thank United Arab Emirates University for providing funding support for this study through a research grant 21F002 (AUA-UAEU grant). Universiti Sains Malaysia RUI grant (1001/CABR/ 8011045) is also acknowledged.
Publisher Copyright:
© 2022 Elsevier Ltd
PY - 2023/2/15
Y1 - 2023/2/15
N2 - This study aims to investigate the potentials of mature (MSPHs) and young (YSPHs) soybean enzymatic protein hydrolysates for the inhibition of pancreatic lipase (PL) and cholesterol esterase (C-Ease) enzymes. Higher proteins degradation levels were recorded with Bromelain compared to Flavourzyme and Alcalase, and upon hydrolysis, improved PL and C-Ease inhibition performances were displayed compared to unhydrolyzed proteins. Afterwards, six PHs with potent anti-lipidemic activities were selected for sequencing using LC-MS QTOF and molecular binding studies. Peptides FPFPRPPHQ, QCCAFEM, FAPEFLK from MSPHs and SFFFPFELPRE, FMYL, PFLL, FPLL, LPHF from YSPHs were predicted to possess potent inhibitory activities against PL. Furthermore, FPFPRPPHQ, FMYL, MMLM from MSPHs, and SFFFPFELPRE from YSPHs were predicted to be potent inhibitors of C-Ease. FPFPRPPHQ and SFFFPFELPRE derived from MSPHs and YSPHs, respectively, demonstrated effective inhibition potentialities against both PL and C-Ease. Therefore, mature and young soybean-derived protein hydrolysates could be recognized as a potential ingredient in the management of hypercholesterolemia.
AB - This study aims to investigate the potentials of mature (MSPHs) and young (YSPHs) soybean enzymatic protein hydrolysates for the inhibition of pancreatic lipase (PL) and cholesterol esterase (C-Ease) enzymes. Higher proteins degradation levels were recorded with Bromelain compared to Flavourzyme and Alcalase, and upon hydrolysis, improved PL and C-Ease inhibition performances were displayed compared to unhydrolyzed proteins. Afterwards, six PHs with potent anti-lipidemic activities were selected for sequencing using LC-MS QTOF and molecular binding studies. Peptides FPFPRPPHQ, QCCAFEM, FAPEFLK from MSPHs and SFFFPFELPRE, FMYL, PFLL, FPLL, LPHF from YSPHs were predicted to possess potent inhibitory activities against PL. Furthermore, FPFPRPPHQ, FMYL, MMLM from MSPHs, and SFFFPFELPRE from YSPHs were predicted to be potent inhibitors of C-Ease. FPFPRPPHQ and SFFFPFELPRE derived from MSPHs and YSPHs, respectively, demonstrated effective inhibition potentialities against both PL and C-Ease. Therefore, mature and young soybean-derived protein hydrolysates could be recognized as a potential ingredient in the management of hypercholesterolemia.
KW - Bioactive peptides
KW - Cholesterol esterase
KW - Hydrolysates
KW - Hypercholesterolemia
KW - Pancreatic lipase
KW - Soybean protein
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U2 - 10.1016/j.foodchem.2022.134192
DO - 10.1016/j.foodchem.2022.134192
M3 - Article
C2 - 36179519
AN - SCOPUS:85138475099
SN - 0308-8146
VL - 402
JO - Food Chemistry
JF - Food Chemistry
M1 - 134192
ER -