Angiotensin I Converting Enzyme-inhibiting Peptides Purified from Elastase-degraded Elastin Prepared from Pig Aorta

Author(s): Iori Maeda*, Shohei Kai, Suguru Taniguchi, Asako Inoue, Hujun Li, Hitoshi Kesamaru, Takeru Nose.

Journal Name: Current Enzyme Inhibition

Volume 14 , Issue 1 , 2018

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Abstract:

Background: Many peptides are produced from food proteins during the manufacturing of various functional foods; unexpected and valuable physiological activities are frequently identified in such released peptides. Elastin, which normally exists as an insoluble elastic fiber, is being used as a new health food material in accordance with the progress in solubilization techniques for elastin.

Objective: To evaluate the usefulness of elastin as a material for functional foods, we prepared highly pure, water-soluble elastin from pig aorta and evaluated its angiotensin-converting enzyme (ACE)- inhibitory activity.

Method: Pure, water-soluble elastin was prepared from pig aorta using a hydrolyzing method employing a hot alkali reagent. Efficient enzymatic degradation of the elastin was achieved by using elastase that is specific for elastin. The ACE-inhibitory activities of elastin and of peptides obtained via enzymatic degradation were investigated. Three novel ACE-inhibiting peptides were purified from the degradation, and we investigated their ACE-inhibitory activities.

Results: Highly pure, water-soluble elastin was prepared from pig aorta; this elastin preparation showed weak inhibitory activity (8.4% inhibition) against ACE. Surprisingly, 6-fold greater enzymeinhibitory activity was observed for elastin peptides obtained from elastase-mediated degradation of the soluble elastin (48.0% inhibition). Among the enzymatically degraded elastin peptides, three were purified and their primary structures were newly characterized as Val-Tyr-Pro-Gly, Val-Gly-Val-Ala- Pro-Gly, and Gly-Tyr-Pro-Ile. All three peptides showed apparent ACE-inhibitory activity, and Val- Tyr-Pro-Gly exhibited the highest inhibitory capacity among them (60.6% inhibition).

Conclusion: These results suggest that water-soluble elastin may serve as a functional food to exert a blood pressure-lowering effect in the body.

Keywords: Amino acid sequence, angiotensin converting enzyme, angiotensin converting enzyme-inhibiting, blood pressure, functional foods, peptides, pig elastin, soluble elastin.

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Article Details

VOLUME: 14
ISSUE: 1
Year: 2018
Page: [67 - 74]
Pages: 8
DOI: 10.2174/1573408013666170912113121

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