Journal article

Activity and bioavailability of food protein-derived angiotensin-I-converting enzyme-inhibitory peptides

Lu Xue, Rongxin Yin, Kate Howell, Pangzhen Zhang

COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY | WILEY | Published : 2021

Abstract

Angiotensin-I-converting enzyme (ACE) inhibitory peptides are able to inhibit the activity of ACE, which is the key enzymatic factor mediating systemic hypertension. ACE-inhibitory peptides can be obtained from edible proteins and have the function of antihypertension. The amino acid sequences and the secondary structures of ACE-inhibitory peptides determine the inhibitory activities and stability. The resistance of ACE-inhibitory peptides to digestive enzymes and peptidase affect their antihypertensive bioactivity in vivo. In this paper, the mechanism of ACE-inhibition, sources of the inhibitory peptides, structure-activity relationships, stability during digestion, absorption and transport..

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Grants

Funding Acknowledgements

This review was supported by the School of Agriculture and Food, Faculty of Veterinary and Agricultural Sciences, The University of Melbourne and College of Biotechnology and Food Science, Tianjin University of Commerce.