Angiotensin-I converting enzyme (ACE) inhibitory peptides from chicken skin gelatin hydrolysate and its antihypertensive effect in spontaneously hypertensive rats


Citation

N. K. Howell, . and N. M. Sarbon, . and W. A. N. Wan Ahmad, . Angiotensin-I converting enzyme (ACE) inhibitory peptides from chicken skin gelatin hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. pp. 903-911. ISSN 2231-7546

Abstract

Chicken skin gelatin hydrolysates and peptides with angiotensin converting enzyme inhibitory (ACEI) activity were produced enzymatically using alcalase pronase E and collagenase before fractionation into 2 5 and 10 kDa fractions. The fraction with the highest ACEI activity was further purified sequentially using gel filtration chromatography RP-HPLC. The ACEI activity of 2 5 and 10 kDa hydrolysate fractions were 69.64 76.80 and 87.69 respectively. Gel filtration chromatography of 2 kDa fraction produced peptides with ACEI activity (92) and showed a similarity to the synthetic drug captopril (93). The relative molecular mass range of the 2 kDa peptide fraction was 300-900 Da comprising mainly Glu H.Pro Gly Ala Pro and Lys. Further separation using HPLC revealed a fraction with the sequence of one peptide: Gly-Pro-Ile-Gly-Pro-Pro-Ser-Gly-Gly-Phe-Asp (IC‚‚ 0.04 mg/mL). The antihypertensive effect of the purified peptide was supported by spontaneously hypertensive rats (SHR). Oral administration of a 15 mg/kg dose of the purified peptide decreased systolic blood pressure significantly for 24 h. These results suggest that the purified peptide derived from chicken skin gelatin hydrolysate has potential antihypertensive properties which can be used as antihypertensive agent in the food and pharmaceutical industries.


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Abstract

Chicken skin gelatin hydrolysates and peptides with angiotensin converting enzyme inhibitory (ACEI) activity were produced enzymatically using alcalase pronase E and collagenase before fractionation into 2 5 and 10 kDa fractions. The fraction with the highest ACEI activity was further purified sequentially using gel filtration chromatography RP-HPLC. The ACEI activity of 2 5 and 10 kDa hydrolysate fractions were 69.64 76.80 and 87.69 respectively. Gel filtration chromatography of 2 kDa fraction produced peptides with ACEI activity (92) and showed a similarity to the synthetic drug captopril (93). The relative molecular mass range of the 2 kDa peptide fraction was 300-900 Da comprising mainly Glu H.Pro Gly Ala Pro and Lys. Further separation using HPLC revealed a fraction with the sequence of one peptide: Gly-Pro-Ile-Gly-Pro-Pro-Ser-Gly-Gly-Phe-Asp (IC‚‚ 0.04 mg/mL). The antihypertensive effect of the purified peptide was supported by spontaneously hypertensive rats (SHR). Oral administration of a 15 mg/kg dose of the purified peptide decreased systolic blood pressure significantly for 24 h. These results suggest that the purified peptide derived from chicken skin gelatin hydrolysate has potential antihypertensive properties which can be used as antihypertensive agent in the food and pharmaceutical industries.

Additional Metadata

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Item Type: Article
AGROVOC Term: Gelatin
AGROVOC Term: Angiotensin
AGROVOC Term: Chickens
AGROVOC Term: Callus (animal skin)
AGROVOC Term: Protein hydrolysate
AGROVOC Term: Experimental animals
AGROVOC Term: Collagenases
AGROVOC Term: Fractionation
AGROVOC Term: Gel filtration chromatography
AGROVOC Term: Peptides
Depositing User: Mr. AFANDI ABDUL MALEK
Last Modified: 24 Apr 2025 00:54
URI: http://webagris.upm.edu.my/id/eprint/8245

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