Keywords
Rice Protein Angiotensin-Converting Enzyme Bioactive Peptides In Vitro Digestion Molecular Weight Distributionrice Protein Angiotensin-Converting Enzyme Bioactive Peptides In Vitro Digestion Molecular Weight Distribution
Abstract
In order to investigate whether the four rice proteins can produce ACE inhibitory active peptides and their activity status after simulated in vitro digestion, this study used rice as raw material and extracted the four rice proteins by the Osborne method. The gastrointestinal digestion process is simulated in vitro to study the production and activity of ACE inhibitory active peptides from digestive enzymatic hydrolysis, and at the same time detect the hydrolysis degree and molecular weight distribution of the enzymatic hydrolysis products. The experimental results showed that after the four rice proteins were digested by pepsin for 30 minutes, the ACE inhibitory activity of the enzymatic hydrolyzate products reached a high level. Subsequently, after the action of trypsin, the ACE inhibitory activity of the enzymatic hydrolyzate products decreased. The half inhibitory concentration IC50 values of 4 h digestion products of rice albumin, globulin, gliadin and glutenin are 1.45 mg/mL, 0.91 mg/mL, 1.19 mg/mL and 0.75 mg/mL respectively, and the molecular weight is concentrated at 1000 u The following are ACE inhibitory active peptides that are easily absorbed by the human body. At the same time, the unenzymatically digested protein has almost no ACE inhibitory activity. The results show that the in vitro digestion enzymatic hydrolysates of the four rice proteins have different ACE inhibitory activities. Among them, the digested products of rice gluten have the highest ACE inhibitory activity. Humans eat rice protein normally and gastrointestinal digestion can produce ACE inhibitory activity that is absorbed by the human body. Active peptides. 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.
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Original research done by Chen Qianqian
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