Activity and bioavailability of food protein-derived angiotensin-I-converting enzyme–inhibitory peptides |
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Authors: | Lu Xue Rongxin Yin Kate Howell Pangzhen Zhang |
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Affiliation: | 1. College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin, China;2. School of Agriculture and Food, Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria, Australia |
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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 transportation of ACE-inhibitory peptides, and consumption of ACE-inhibitory peptides are reviewed, which provide guidance to the development of new functional foods and production of antihypertensive nutraceuticals and pharmaceuticals. |
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Keywords: | ACE-inhibitory peptides bioaccessibility bioavailability functional food protein structure–activity relationship |
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