Angiotensin I-converting enzyme, dipeptidyl peptidase-IV, and alpha-glucosidase inhibitory potential of hazelnut meal protein hydrolysates

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dc.authorscopusid16305343200
dc.contributor.authorSimsek, Sebnem
dc.date.accessioned2023-01-12T19:51:04Z
dc.date.available2023-01-12T19:51:04Z
dc.date.issued2021
dc.departmentN/A/Departmenten_US
dc.description.abstractThe objective of this study was to determine the bioactive potential of hazelnut meal protein hydrolysates. Hazelnut meal protein isolate was hydrolyzed using Alcalase and Trypsin + Chymotrypsin to 23.5% and 13.7% degrees of hydrolysis, respectively. The peptide fractions (< 5 kDa and > 5 kDa) were screened for the in vitro inhibition of angiotensin I-converting enzyme (ACE), dipeptidyl peptidase-IV (DPP-IV), and alpha-glucosidase activities. Peptide fractions > 5 kDa showed a higher potency to inhibit ACE (IC50 = 0.10-0.13 mg/mL), whereas peptide fractions < 5 kDa were more effective in inhibiting DPP-IV (IC50 = 0.37-0.45 mg/mL) and alpha-glucosidase (IC50 =3.62-3.89 mg/mL), with no significant difference in treatment with Alcalase and Trypsin + Chymotrypsin. The results of the study showed that hazelnut meal protein is a potential source of bioactive peptide delivery and that the hydrolysates obtained could be used as an alternative ingredient for the development of new functional foods.en_US
dc.description.sponsorshipEge University Scientific Research Council [15-MUH-065]en_US
dc.description.sponsorshipI would like to thank Ege University Scientific Research Council for their financial support (Project number: 15-MUH-065).en_US
dc.identifier.doi10.1007/s11694-021-00994-8
dc.identifier.endpage4496en_US
dc.identifier.issn2193-4126
dc.identifier.issn2193-4134
dc.identifier.issn2193-4126en_US
dc.identifier.issn2193-4134en_US
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85108587198en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage4490en_US
dc.identifier.urihttps://doi.org/10.1007/s11694-021-00994-8
dc.identifier.urihttps://hdl.handle.net/11454/76214
dc.identifier.volume15en_US
dc.identifier.wosWOS:000664450700002en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofJournal Of Food Measurement And Characterizationen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAngiotensin I-converting enzymeen_US
dc.subjectDipeptidyl peptidase-IVen_US
dc.subjectalpha-glucosidaseen_US
dc.subjectHazelnut mealen_US
dc.subjectProtein hydrolysateen_US
dc.subjectChenopodium-Quinoa Willd.en_US
dc.subjectBioactive Peptidesen_US
dc.subjectAceen_US
dc.subjectVitroen_US
dc.subjectIdentificationen_US
dc.subjectPurificationen_US
dc.subjectPressureen_US
dc.subjectAmylaseen_US
dc.titleAngiotensin I-converting enzyme, dipeptidyl peptidase-IV, and alpha-glucosidase inhibitory potential of hazelnut meal protein hydrolysatesen_US
dc.typeArticleen_US

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