Antioxidative Peptides and Angiotensin I-converting Enzyme Inhibitory Peptides Obtained from Soybean by Protease Treatment at Pilot Scale
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Abstract:
A pilot-scale production of soybean oligopeptides (SOPs) was developed in this study, and the SOPs had a high protein content (91.45%) and low molecular weight (84.37% of the product were less than 1000 u). The in vitro antioxidant activity and angiotensin I-converting enzyme (ACE) inhibitory activity of SOPs were analyzed. SOPs were then separated by reversed-phase high performance liquid chromatography, and six major fractions (numbered from 1?6) were collected and subjected to mass spectrometry to identify the active peptides. The sequences of 41 peptide fragments were identified, and 15 peptide fragments were selected to evaluate the antioxidative and ACE inhibitory activities using the aforementioned methods. The results showed that SOPs contained two novel potent antioxidative peptide fragments (Tyr-Glu, 8.61 ± 0.42 mmol Trolox equivalents/g sample; Asp-Tyr-Arg, 6.53 ± 0.34 mmol Trolox equivalents/g sample) and four potent ACE inhibitory peptide fragments (Leu-Val-Arg, IC50 = 51.75 μM; Leu-Tyr, IC50 = 305.76 μM; Asp-Tyr-Arg, IC50 = 1082.95 μM; Asp-Phe, IC50 = 1106.04 μM). Most of them were novel antioxidant or ACE inhibitory peptides derived from soybeans. This study suggested that SOPs and their active peptides might be used as antioxidative or hypotensive substances in food additives, dietary nutrients, and pharmaceutical agents.
