TY - JOUR
T1 - Amaranth proteins as potential source of bioactive peptides with enhanced inhibition of enzymatic markers linked with hypertension and diabetes
AU - Kamal, Hina
AU - Mudgil, Priti
AU - Bhaskar, Bincy
AU - Fisayo, Ajayi Feyisola
AU - Gan, Chee Yuen
AU - Maqsood, Sajid
N1 - Funding Information:
Authors are thankful to United Arab Emirates University for funding this research through a research grants ( AUA-12F002 ) awarded to Sajid Maqsood. University Sains Malaysia RUI grant ( 1001/CABR/ 8011045 ) to Chee-Yuen Gan is also acknowledged.
Publisher Copyright:
© 2021 Elsevier Ltd
PY - 2021/9
Y1 - 2021/9
N2 - The health and environmental concerns are provoking changes in human diets and plant-based proteins are being considered as sustainable source of proteins compared to animal-derived proteins. In line with this, the current study investigated amaranth protein isolate (API) and hydrolysates (APHs) for in-vitro angiotensin-I converting enzyme (ACE), dipeptidyl peptidase-IV (DPP-IV), and α-glucosidase (AG) inhibitory activities. Amaranth protein hydrolysates (APHs) were generated by bromelain, chymotrypsin, and pronase E for 2, 4, and 6 h. All APHs, especially bromelain-4 h hydrolysate (B4) displayed enhanced ACE, DPP-IV, and AG inhibition compared to API and other APHs. About 116 peptides were identified in B4 by LC-MS-QToF and 17 peptides were predicted to be bioactive. Six of these peptides were predicted to possess high ACE inhibiting potential, while peptides FPFPPTLGY and FPFPR were found to bind to the highest number of active hotspots of DPP-IV and AG, respectively. Overall, this study demonstrated that APHs could be a potential source of antidiabetic and antihypertensive peptides for functional food formulation.
AB - The health and environmental concerns are provoking changes in human diets and plant-based proteins are being considered as sustainable source of proteins compared to animal-derived proteins. In line with this, the current study investigated amaranth protein isolate (API) and hydrolysates (APHs) for in-vitro angiotensin-I converting enzyme (ACE), dipeptidyl peptidase-IV (DPP-IV), and α-glucosidase (AG) inhibitory activities. Amaranth protein hydrolysates (APHs) were generated by bromelain, chymotrypsin, and pronase E for 2, 4, and 6 h. All APHs, especially bromelain-4 h hydrolysate (B4) displayed enhanced ACE, DPP-IV, and AG inhibition compared to API and other APHs. About 116 peptides were identified in B4 by LC-MS-QToF and 17 peptides were predicted to be bioactive. Six of these peptides were predicted to possess high ACE inhibiting potential, while peptides FPFPPTLGY and FPFPR were found to bind to the highest number of active hotspots of DPP-IV and AG, respectively. Overall, this study demonstrated that APHs could be a potential source of antidiabetic and antihypertensive peptides for functional food formulation.
KW - ACE
KW - Amaranth
KW - Antidiabetic peptides
KW - Antihypertensive
KW - DPP-IV
KW - Protein hydrolysates
KW - α-glucosidase
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U2 - 10.1016/j.jcs.2021.103308
DO - 10.1016/j.jcs.2021.103308
M3 - Article
AN - SCOPUS:85112484705
SN - 0733-5210
VL - 101
JO - Journal of Cereal Science
JF - Journal of Cereal Science
M1 - 103308
ER -