Molecular docking studies on α-amylase inhibitory peptides from milk of different farm animals
dc.contributor.author | Mudgil, P | |
dc.contributor.author | Al Dhaheri, MKO | |
dc.contributor.author | Alsubousi, MSM | |
dc.contributor.author | Khan, H | |
dc.contributor.author | Redha, AA | |
dc.contributor.author | Yap, P-G | |
dc.contributor.author | Gan, C-Y | |
dc.contributor.author | Maqsood, S | |
dc.date.accessioned | 2024-05-03T09:29:07Z | |
dc.date.issued | 2023-12-14 | |
dc.date.updated | 2024-04-25T18:52:36Z | |
dc.description.abstract | Milk-derived peptides have emerged as a popular mean to manage various lifestyle disorders such as diabetes. Fermentation is being explored as one of the faster and efficient way of producing peptides with antidiabetic potential. Therefore, in this study, an attempt was made to comparatively investigate the pancreatic α-amylase (PAA) inhibitory properties of peptides derived from milk of different farm animals through probiotic fermentation. Peptide's identification was carried out using liquid chromatography-quadrupole time-of-flight mass spectrometry and inhibition mechanisms were characterized by molecular docking. Results obtained showed a PAA-IC50 value (the amount of protein equivalent needed to inhibit 50% of enzymes) between 2.39 and 36.1 µg protein equivalent for different fermented samples. Overall, Pediococcus pentosaceus MF000957-derived fermented milk from all animals indicated higher PAA inhibition than other probiotic derived fermented milk (PAA-IC50 values of 6.01, 3.53, 15.6, and 10.8 µg protein equivalent for bovine, camel, goat, and sheep fermented milk). Further, molecular docking analysis indicated that camel milk-derived peptide IMEQQQTEDEQQDK and goat milk-derived peptide DQHQKAMKPWTQPK were the most potent PAA inhibitory peptides. Overall, the study concluded that fermentation derived peptides may prove useful in for managing diabetes via inhibition of carbohydrate digesting enzyme PAA. | en_GB |
dc.description.sponsorship | United Arab Emirates University | en_GB |
dc.format.extent | 2633-2652 | |
dc.identifier.citation | Vol. 107(5), pp. 2633-2652 | en_GB |
dc.identifier.doi | https://doi.org/10.3168/jds.2023-24118 | |
dc.identifier.grantnumber | SURE Plus–G00002836 | en_GB |
dc.identifier.uri | http://hdl.handle.net/10871/135841 | |
dc.language.iso | en | en_GB |
dc.publisher | Elsevier / American Dairy Science Association | en_GB |
dc.rights | © 2024, The Authors. Published by Elsevier Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/ | en_GB |
dc.subject | antidiabetic bioactive peptides | en_GB |
dc.subject | milk fermentation | en_GB |
dc.subject | molecular docking | en_GB |
dc.subject | probiotics | en_GB |
dc.subject | α-amylase inhibition | en_GB |
dc.title | Molecular docking studies on α-amylase inhibitory peptides from milk of different farm animals | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2024-05-03T09:29:07Z | |
dc.identifier.issn | 0022-0302 | |
exeter.place-of-publication | United States | |
dc.description | This is the final version. Available on open access from Elsevier via the DOI in this record | en_GB |
dc.identifier.eissn | 1525-3198 | |
dc.identifier.journal | Journal of Dairy Science | en_GB |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | en_GB |
dcterms.dateAccepted | 2023-11-20 | |
rioxxterms.version | VoR | en_GB |
rioxxterms.licenseref.startdate | 2023-12-14 | |
rioxxterms.type | Journal Article/Review | en_GB |
refterms.dateFCD | 2024-05-03T09:25:31Z | |
refterms.versionFCD | VoR | |
refterms.dateFOA | 2024-05-03T09:29:14Z | |
refterms.panel | A | en_GB |
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Except where otherwise noted, this item's licence is described as © 2024, The Authors. Published by Elsevier Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/