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

[ Vol. 14 , Issue. 1 ]

Author(s):

Iori Maeda*, Shohei Kai, Suguru Taniguchi, Asako Inoue, Hujun Li, Hitoshi Kesamaru and Takeru Nose   Pages 67 - 74 ( 8 )

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.

Affiliation:

Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Department of Chemistry, Faculty and Graduate School of Science, Kyushu University, Fukuoka 812-8581, Department of Chemistry, Faculty and Graduate School of Science, Kyushu University, Fukuoka 812-8581

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