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- W2948183118 abstract "Antioxidant and angiotensin-I converting enzyme inhibitory (ACE-I) activities of bioactive peptide fractions from camel milk fermented by Leuconostoc lactis PTCC 1899 were assessed. The fraction <3 kDa obtained from ultrafiltration showed ACE-I (IC50 = 1.61 ± 0.18 mg mL−1) and ABTS radical scavenging (1883.39 μm TE mg−1 protein) activities and was purified through RP-HPLC. The active peptide, MVPYPQR, with antioxidant (8933.05 μm TE mg−1 peptide) and ACE-I (IC50 = 30 μm) activities was identified. To investigate the ACE-I mechanism of the purified peptide the docking study was performed. The presence of hydrogen bond between Gln 162 (S'1 pocket of ACE) and Arg in the C terminal of the peptide was identified and the peptide could distort the Zn2+ tetrahedral geometry of the enzyme. This study showed the ability of Leuc. lactis to produce a novel and safe functional food by hydrolysing the milk proteins during the fermentation." @default.
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- W2948183118 date "2019-10-01" @default.
- W2948183118 modified "2023-10-18" @default.
- W2948183118 title "Novel β-casein derived antioxidant and ACE-inhibitory active peptide from camel milk fermented by Leuconostoc lactis PTCC1899: Identification and molecular docking" @default.
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- W2948183118 doi "https://doi.org/10.1016/j.idairyj.2019.05.012" @default.
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