Novel Angiotensin I-converting enzyme inhibitory peptides found in a thermolysin-treated elastin with antihypertensive activity |
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Authors: | Yuko Sato Tsudoi Toyoda Akiko Shimizu-Ibuka Tomoko Tamura Kazuo Kobayashi-Hattori Takemichi Nakamura Soichi Arai Kiyoshi Mura |
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Affiliation: | Department of Nutrition and Dietetics, Faculty of Family and Consumer Sciences, Kamakura Women's University, Kamakura, Kanagawa, Japan. |
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Abstract: | Angiotensin I-converting enzyme (ACE) inhibitory activity was generated from elastin and collagen by hydrolyzing with thermolysin. The IC50 value of 531.6 μg/mL for ACE inhibition by the elastin hydrolysate was five times less than 2885.1 μg/mL by the collagen hydrolysate. We confirmed the antihypertensive activity of the elastin hydrolysate in vivo by feeding spontaneously hypertensive rats (male) on a diet containing 1% of the elastin hydrolysate for 9 weeks. About 4 week later, the systolic blood pressure of the rats in the elastin hydrolysate group had become significantly lower than that of the control group. We identified novel ACE inhibitory peptides, VGHyp, VVPG and VYPGG, in the elastin hydrolysate by using a protein sequencer and quadrupole linear ion trap (QIT)-LC/MS/MS. VYPGG had the highest IC50 value of 244 μM against ACE and may have potential use as a functional food. |
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