Abstract: The angiotensin convert enzyme peptides (ACE) inhibitor peptides were purified from enzymatic hydrolysate of soft part excluding adductors of yesso scallopPatinopectenyessoensis by gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC),and then the structure and hypertensive activity of the ACE inhibitor peptides were studied. The fractions F5 and F7 separated by Sephadex LH-20 were shown to inhibit ACE, with 50% inhibitory concentration (IC50) of 1.4 mg/mL for F5 and 1.7 mg/mL for F7. The F5-3-3 was derived from F5-3 with RP-HPLC for twice, and the peptide Val-Trp (VW) identified by mass spectrometry (MS) had ACE inhibition, with IC50 of 86.9 μmol/L. Then the enzymic hydrolysate with molecular weight of below 3000 obtained by filtration was gavaged to spontaneously hypertensive rat (SHR) for 28 days when very significantly decrease in systolic blood pressure (SBP) was observed in SHR (P<0.01), even very significantly lower(systolic pressure of 172 mmHg)than that in the control group 9 days after intragastric administration(P<0.01). The findings indicate that the enzymic hydrolysate from soft part excluding adductors of yesso scallop has a role in reduction in blood pressure and becomes a candidate for development of hypoglycemic drugs and health food.
李晶晶, 尤海琳, 张亚飞, 李敏, 赵慧, 胡建恩, 卢航. 扇贝裙边ACE抑制肽的分离鉴定及其降血压活性研究[J]. 大连海洋大学学报, 2018, 33(6): 782-787.
LI Jing-jing, YOU Hai-lin, ZHANG Ya-fei, LI Min, ZHAO Hui, HU Jian-en, LU Hang. Isolation,purification and hypotensive activity determination of ACE inhibitor peptides derived from soft part excluding adductors of yesso scallop. Journal of Dalian Ocean University, 2018, 33(6): 782-787.