The objective of this study was to determine the in vitro antioxidant and antihypertensive potentials of sesame seed protein hydrolysate and its membrane ultrafiltration peptide fractions in comparison to the unhydrolyzed protein. Sesame seed protein isolate (SESPI) was prepared from the defatted sesame seed meal and then hydrolyzed using consecutive additions of pepsin and pancreatin to yield sesame protein hydrolysate (SESPH). The SESPH was subjected to membrane ultrafiltration consecutively to obtain fractions with peptide sizes of <1, 1-3, 3-5, and 5-10 kDa, respectively, which were then assayed for in vitro antioxidant and antihypertensive properties. The results showed that protein hydrolysis and fractionation led to significant (p < .05) increases in the content of hydrophobic amino acids. Radical scavenging and metal ion chelation were also significantly (p < .05) enhanced by these treatments. Inhibition of linoleic acid oxidation was stronger with the 1.0 mg/ml of sesame peptide samples in comparison to the mild inhibitory effect exhibited by the 0.5 mg/ml of samples. The <1 kDa peptide fraction was the most active inhibitor (81%) against angiotensin converting enzyme, whereas the bigger peptides (>3-5 and 5-10 kDa) were the most effective (75%-85% ) inhibitors against renin. These sesame products could be used as therapeutic agents in the development of health enhancing foods for the prevention and management of chronic diseases. PRACTICAL APPLICATIONS: Bioactive peptides have been produced from plant protein sources through in vitro enzymatic activities. Sesame seed peptides have demonstrated multifunctional potential to act as antioxidative and antihypertensive agents that could be utilized as ingredients for the development of novel functional foods and nutraceuticals.
Keywords: angiotensin converting enzyme; antioxidants; membrane ultrafiltration; protein hydrolysate; renin; sesame seed.
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