Purification and Identification of Three novel angiotensin-I-converting inhibitory Peptides from Acetes chinensis hydrolysate
Acetes chinensis obtained from Bo Hai Gulf is a valuable protein source. It was digested by protease produced by Bacillus sp. SM98011. The angintensin I-converting enzyme (ACE) inhibitory activity of hydrolysate was investigated. IC50 value of hydrolysate was 0.98mg/ml. IC50 value of the ultrafiltrate of the hydrolysate with MW cut-off 3000 KDa increased up to 0.22 mg/ml. Peptide fractions in the ultrafiltrate was separated with Sephadex G-15 gel chromatography. The most potent fractions were fractionated by reverse-phase high-performance liquid chromatography (HPLC). The three new inhibitory peptides for ACE were purified and sequenced after successive chromatographic isolation. They were Phe-Cys-Val-Leu-Arg-Pro, Ile-Phe-Val-Pro-Ala-Phe and Lys-Pro-Pro-Glu-Thr-Val, with IC50 values of 13.4 礛, 3.2 礛 and 24.1 礛, respectively. The results demonstrate that Acetes chinensis was a promising protein source for the production of ACE inhibitory peptides ,which can be used as materials for antihypertensive functional foods.
转换酶 羊草菜 超滤液 降血压肽
Li Yu Zong
State Key Lab of Microbial Technology,Shandong University,Jinan,250100,China
国内会议
全国首届海洋生物化学与分子生物学学术会议暨全国第五届海洋生命活性物质与天然生化药物学术研讨会
湖北宜昌
英文
268-275
2004-05-28（万方平台首次上网日期，不代表论文的发表时间）