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

作者：Gu Rui Zeng; Liu Wen Ying; Lin Feng; Jin Zhen Tao; Chen Liang; Yi Wei Xue; Lu Jun; Cai Mu Yi^*

来源：Food Research International, 2012, 49(1): 326-333.

DOI：10.1016/j.foodres.2012.07.009

• Black-bone silky fowl
• Enzymatic hydrolysis
• Low-molecular-weight peptides
• Antioxidant activity
• ACE inhibitory activity

Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4 L 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 +/- 0.11 mmol Trolox equivalents/g sample) and two novel potent ACE inhibitory peptides (Leu-Glu-Arg, IC50 = 45.62 +/- 2.40 mu M; Gly-Ala-Gly-Pro, IC50 = 253.07 +/- 6.66 mu M) were found. Their activities were approximately 6.9, 14.1 and 2.8 times higher than that of BSFP, respectively.

• 出版日期2012-11
• 单位中国食品发酵工业研究院