| Résumé | This work aimed to determine the antioxidant properties of identified hydrolyzed oat proteins and peptides, and their capacity to inhibit lipase and α-amylase. The protein hydrolysates retarded the oxidation of peanut oil by reducing peroxide values (up to 2.5-fold), relative to the control oil. Of the five tested peptides, P1 (YFDEQNEQFR), P3 (SPFWNINAH), and P4 (NINAHSVVY) significantly reduced the oxidation of linoleic acid. In the enzyme assays, P3 was the best lipase inhibitor (IC₅₀ 85.4 ± 3 µM) while P1 was the most potent inhibitor of α-amylase (IC₅₀ 37.5 ± 1.1 µM). The structure–activity relationship assessed using the CABS-dock computational model predicted that interactions between peptides and pancreatic lipase residues of Ser¹⁵³, His²⁶⁴, and Asp¹⁷⁷ were important for the inhibition. In the case of α-amylase, interactions with residues of the active sites (Asp¹⁹⁷, Glu²³³, and Asp³⁰⁰), but not those of calcium- or chloride-binding domains, were important for the inhibition.IC |
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