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

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

Volume: 14 Issue: 1

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

Affiliation:

• Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502,Japan

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

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.

Cite this article as:

Maeda Iori *, Kai Shohei , Taniguchi Suguru , Inoue Asako , Li Hujun , Kesamaru Hitoshi and Nose Takeru , Angiotensin I Converting Enzyme-inhibiting Peptides Purified from Elastase-degraded Elastin Prepared from Pig Aorta, Current Enzyme Inhibition 2018; 14 (1) . https://dx.doi.org/10.2174/1573408013666170912113121

DOI https://dx.doi.org/10.2174/1573408013666170912113121	Print ISSN 1573-4080
Publisher Name Bentham Science Publisher	Online ISSN 1875-6662