Abstract
The 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 α-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 α-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.
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I would like to thank Ege University Scientific Research Council for their financial support (Project number: 15-MUH-065).
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Simsek, S. Angiotensin I-converting enzyme, dipeptidyl peptidase-IV, and α-glucosidase inhibitory potential of hazelnut meal protein hydrolysates. Food Measure 15, 4490–4496 (2021). https://doi.org/10.1007/s11694-021-00994-8
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DOI: https://doi.org/10.1007/s11694-021-00994-8