Classification and Antihypertensive Activity of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Food Proteins

• Published in: Journal of food science Vol. 65; no. 4; pp. 564 - 569
• Main Authors: Iroyukifujita, H, Eiichiyokoyama, K, Yoshikawa, Masaaki
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.05.2000; Institute of Food Technologists; Wiley Subscription Services, Inc
• Subjects: Analytical, structural and metabolic biochemistry; angiotensin I-converting enzyme inhibitor; Biological and medical sciences; bonito; chicken muscle; Coenzymes, vitamins; Enzymes; Food industries; Food science; Fundamental and applied biological sciences. Psychology; Other biological molecules; ovalbumin; Peptides; Proteins; Research and development. New food products, dietetic foods and beverages; spontaneously hypertensive rat; Enzymatic treatment; Intravenous administration; Peptides; Rat; Peptidyl-dipeptidase A; Muscle; Blood pressure; Aves; Ovalbumin; Enzyme; Rodentia; Oral administration; Enzyme inhibitor; Foodstuff; In vitro; Biological activity; Peptidases; In vivo; Vertebrata; Mammalia; Animal; Enzymatic digestion; Hydrolases; Peptidyl-dipeptidases; Antihypertensive agent; Chicken
• ISSN: 0022-1147; 1750-3841
• DOI: 10.1111/j.1365-2621.2000.tb16049.x

Angiotensin I‐converting enzyme (ACE)‐inhibitory peptides from the thermolysin digest of chicken muscle and the peptic digest of ovalbumin were isolated. However, some of them failed to show antihypertensive activity in spontaneously hypertensive rats (SHR). To clarify this discrepancy, ACE‐inhibitory peptides from various sources were preincubated with ACE before measurement of ACE‐inhibitory activity and classified into 3 groups: (1) inhibitor type, IC50 values of peptides that are not affected after preincubation with ACE; (2) substrate type, peptides that are hydrolyzed by ACE to give peptides with weaker activity; and (3) prodrug‐type inhibitor, these peptides are converted to true inhibitors by ACE or gastrointestinal proteases. Peptides belonging to the 1st and the 3rd groups exert antihypertensive activities even after oral administration in SHR.