Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle

Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE)...

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Bibliographic Details
Published in:Food research international 2012-11, Vol.49 (1), p.326-333
Main Authors: Gu, Rui-Zeng, Liu, Wen-Ying, Lin, Feng, Jin, Zhen-Tao, Chen, Liang, Yi, Wei-Xue, Lu, Jun, Cai, Mu-Yi
Format: Article
Language:English
Subjects:
ACE inhibitory activity
Antioxidant activity
Antioxidants
Biological and medical sciences
Black-bone silky fowl
chickens
Enzymatic hydrolysis
Enzymes
Equivalence
Food industries
Foods
Fundamental and applied biological sciences. Psychology
Gallus gallus
Low-molecular-weight peptides
mass spectrometry
molecular weight
Muscles
oligopeptides
papain
Peptides
peptidyl-dipeptidase A
Radicals
reversed-phase high performance liquid chromatography
Scavenging
subtilisin
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Summary:Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. BSFP was then separated by reversed-phase high performance liquid chromatography. Five major fractions were collected and their 2,2′-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging and ACE inhibitory activities were assayed. Fractions 3–5 displaying higher activities were subjected to mass spectrometry to identify the active peptides. A total of 29 peptide sequences were identified, and 11 peptides were synthesized for further ABTS radical scavenging and ACE inhibitory activity analysis. Finally, one potent antioxidative peptide (Leu-Trp-Arg, 3.25±0.11mmol Trolox equivalents/g sample) and two novel potent ACE inhibitory peptides (Leu-Glu-Arg, IC50=45.62±2.40μM; Gly-Ala-Gly-Pro, IC50=253.07±6.66μM) were found. Their activities were approximately 6.9, 14.1 and 2.8 times higher than that of BSFP, respectively. ► We describe a practical way to utilize black-bone silky fowl muscle. ► One potent antioxidant peptide is identified from the hydrolysate. ► Two novel potent ACE inhibitory peptides are identified from the hydrolysate.
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2012.07.009