期刊
JOURNAL OF FOOD SCIENCE
卷 79, 期 1, 页码 C1-C7出版社
WILEY
DOI: 10.1111/1750-3841.12269
关键词
angiotensin I-converting enzyme inhibitory peptide; blood pressure; purification; ribbonfish backbone
资金
- Natl. Natural Science Foundation of China [31130042]
- Program for New Century Excellent Talents in Univ. [NCET-10-0698]
- Zhejiang Provincial Natural Science Foundation [Y2111237]
- Natural Science and Engineering Research Council of Canada (NSERC)
Ribbonfish (Trichiurus haumela) backbone is normally discarded as an industrial waste from fish processing. A method of developing angiotensin I-converting enzyme inhibitory (ACEI) peptides from ribbonfish backbone was previously optimized. The purposes of the study were to characterize the active peptides in the hydrolysate and to evaluate its in vivo activity. Ribbonfish backbone protein hydrolysate prepared by acid protease was fractionated into 4 fractions (I, MW< 1 kDa; II, MW= 1 to 5 kDa; III, MW= 5 to 10 kDa; and IV, MW> 10 kDa) through ultrafiltration membranes. Fraction I, showing the highest ACEI activity, was further purified using consecutive chromatographic techniques including gel filtration and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide was determined to have a molecular weight of 317.25 Da, with a sequence of Leu-Trp and an IC50 value of 5.6M. Systolic blood pressure of spontaneously hypertensive rats was significantly decreased from 181 2.0 to 161.3 +/- 2.3mm Hg after 4h of oral administration of Leu-Trp at a dose of 10mg/kg of body weight. These results indicated that ribbonfish backbone protein could be used for development of antihypertensive agent.
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