Angiotensin I converting enzyme-inhibiting peptides purified from elastase-degraded elastin prepared from pig aorta

Iori Maeda, Shohei Kai, Suguru Taniguchi, Asako Inoue, Hujun Li, Hitoshi Kesamaru, Takeru Nose

Research output: Contribution to journalArticle

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 enzyme-inhibitory 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.

Original languageEnglish
Pages (from-to)67-74
Number of pages8
JournalCurrent Enzyme Inhibition
Volume14
Issue number1
DOIs
Publication statusPublished - Apr 1 2018

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Elastin
Pancreatic Elastase
Peptidyl-Dipeptidase A
Aorta
Swine
Peptides
Enzyme activity
Functional Food
Degradation
Water
Food
Elastic Tissue
Pressure effects
Blood pressure
Alkalies

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Drug Discovery

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Angiotensin I converting enzyme-inhibiting peptides purified from elastase-degraded elastin prepared from pig aorta. / Maeda, Iori; Kai, Shohei; Taniguchi, Suguru; Inoue, Asako; Li, Hujun; Kesamaru, Hitoshi; Nose, Takeru.

In: Current Enzyme Inhibition, Vol. 14, No. 1, 01.04.2018, p. 67-74.

Research output: Contribution to journalArticle

Maeda, Iori ; Kai, Shohei ; Taniguchi, Suguru ; Inoue, Asako ; Li, Hujun ; Kesamaru, Hitoshi ; Nose, Takeru. / Angiotensin I converting enzyme-inhibiting peptides purified from elastase-degraded elastin prepared from pig aorta. In: Current Enzyme Inhibition. 2018 ; Vol. 14, No. 1. pp. 67-74.
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AU - Maeda, Iori

AU - Kai, Shohei

AU - Taniguchi, Suguru

AU - Inoue, Asako

AU - Li, Hujun

AU - Kesamaru, Hitoshi

AU - Nose, Takeru

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AB - 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 enzyme-inhibitory 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.

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