AI Article Synopsis
- ACE inhibitory activity was derived from elastin and collagen using thermolysin, showing that elastin hydrolysate was significantly more effective (IC50 of 531.6 µg/mL) compared to collagen (IC50 of 2885.1 µg/mL).
- In vivo tests on hypertensive rats revealed that those fed a diet with 1% elastin hydrolysate for 9 weeks experienced a notable decrease in systolic blood pressure compared to controls after 4 weeks.
- Novel ACE inhibitory peptides, including VGHyp, VVPG, and VYPGG, were identified in the elastin hydrolysate, with VYPGG showing the highest inhibitory potential (IC50 of 244 µM),
Article 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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| http://dx.doi.org/10.1271/bbb.120083 | DOI Listing |
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