Angiotensin-converting Enzyme Inhibition By Rice Protein Hydrolysate
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Abstract:
In this study, the production of peptides with angiotensin-converting enzyme (ACE) inhibition activity was investigated from simulated in vitro digestion of four rice proteins, namely albumin, globulin, prolamin, and glutelin. The proteins were extracted from rice using the Osborne method. Production and ACE inhibiting activity, the degree of hydrolysis, and the molecular weight distribution of the proteolysis products were investigated. The results revealed that ACE inhibition activity of individual products obtained after proteolysis of the proteins, was high after 30 min of pepsin digestion. The activity decreased upon subsequent digestion with trypsin. The hydrolysates of rice albumin, globulin, prolamin, and glutelin after 4-hour digestion showed half-inhibition concentration (IC50) of 1.45, 0.91, 1.19, and 0.75 mg/mL, respectively, and their molecular weight was < 1000 u, which means they can be easily absorbed by the human body. At the same time, undigested proteins had almost no ACE inhibition activity. The result also showed the products of in vitro protein proteolysis had different ACE inhibition activities and that rice glutelin proteolysis product showed the highest ACE inhibition activity. Therefore, the gastrointestinal digestion of regularly consumed rice can produce ACE-inhibiting peptides that can be absorbed by the human body.
