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Antihypertensive activity of orally consumed ACE-I inhibitory peptides

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Pages 8986-8999 | Published online: 02 Jul 2021
 

Abstract

Food proteins are sources for ACE-I inhibitory peptides that can be extracted by enzymatic hydrolysis exhibiting anti-hypertensive activity. However, these peptides are prone to further degradation by gastrointestinal enzymes during oral consumption. Bio-activity of these peptides is dependent on the resultant peptide post gastrointestinal digestion. To exhibit the bio-activity, they need to be absorbed in intact form. Although studies suggest di and tri-peptides show better ACE-I inhibitory activity, few peptides show altered IC50 values under simulated gastrointestinal digestion. Moreover, ACE-I inhibitory peptides with low IC50 values have not shown effective anti-hypertensive activity in spontaneously hypertensive rats when administered orally. Few ACE-I inhibitory peptides have reported effective reduction in systolic blood-pressure when administered through intravenously. During oral consumption of such peptides, the actual peptide sequence responsible for reducing blood-pressure is a result of breakdown in gastrointestinal tract. The fate of targeted peptides during digestion depends on amino acid sequence of the protein containing the specific site for cleavage where the action of digestive enzymes takes place. Therefore, this review attempts to explain the factors that affect the anti-hypertensive activity of ACE-I inhibitory peptides during oral consumption. It also highlights subsequent absorption of ACE-I inhibitory peptides after gastrointestinal digestion.

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Acknowledgement

The authors thank to Dr. Anirban Chakraborty, Director, Nitte (Deemed to be University), Nitte University Centre for Science Education and Research. The authors extend sincere thanks to Mr. K.K Bhat, Former HOD, Department of Sensory Science, CFTRI, Mysore for valuable suggestions. The authors also thank Dr. Iddya Karunasagar and Dr. Indrani Karunasagar, DST-NUTEC, Nitte (Deemed to be University) for their constant support. The authors thanks Nitte (Deemed to be University) for funding the above work.

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