Simsek, Sebnem2023-01-122023-01-1220212193-41262193-41342193-41262193-4134https://doi.org/10.1007/s11694-021-00994-8https://hdl.handle.net/11454/76214The 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.en10.1007/s11694-021-00994-8info:eu-repo/semantics/closedAccessAngiotensin I-converting enzymeDipeptidyl peptidase-IValpha-glucosidaseHazelnut mealProtein hydrolysateChenopodium-Quinoa Willd.Bioactive PeptidesAceVitroIdentificationPurificationPressureAmylaseArticle15544904496WOS:0006644507000022-s2.0-85108587198Q2Q3