title: Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis.
abstract: Acetes chinensis is an underutilized shrimp species thriving in the Bo Hai Gulf of China. In a previous study, we had used the protease from Bacillus sp. SM98011 to digest this kind of shrimp and found that the oligopeptide-enriched hydrolysate possessed antioxidant activity and high angiotensin I-converting enzyme (ACE) inhibitory activity with an IC50 value of 0.97 mg/ml. In this paper, by ultrafiltration, gel permeation chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC), five peptides with high ACE inhibitory activity were purified from the shrimp hydrolysates and their sequences were identified by amino acid composition analysis and molecular weight (MW) analysis. Three of them, FCVLRP (a), IFVPAF (f) and KPPETV (j), were novel ACE inhibitory peptides. Their IC50 values were 12.3 microM, 3.4 microM and 24.1 microM, respectively, and their recoveries were 30 mg/100 g (solid basis of shrimp), 19 mg/100 g and 33 mg/100 g, respectively. Lineweaver-Burk plots for the three novel peptides showed that they are all competitive inhibitors. To test the ACE inhibitory activity of peptide a, f, j after they were digested by digestive enzymes in vivo, 12 derived peptides from FCVLRP and IFVPAF were synthesized based on their amino acid sequences and the cleavage sites of digestive enzymes. No digestive enzyme cleavage site was found in KPPETV. The IC50 values of the derived peptides were determined and the result showed that except for VPAF, FC and FCVL, the ACE inhibitory activity of the other nine derived peptides did not significantly change when compared with their original peptides. Surprisingly, five peptides had lower IC50 values than their original peptides, particularly for RP (IC50 value = 0.39 microM), which is about 30 times lower than its original peptide and almost the lowest IC50 value for ACE inhibitory peptides reported. Therefore, the novel peptides identified from A. chinensis hydrolysates probably still maintain a high ACE inhibitory activity even if they are digested in vivo. This is the first report about novel ACE inhibitory peptides from hydrolysates of marine shrimp A. chinensis. The novel peptides from hydrolysate of A. chinensis and some of their derived peptides with high ACE inhibitory activity probably have potential in the treatment of hypertension or in clinical nutrition.
authors.affiliation: State Key Lab of Microbial Technology, Shandong University, Jinan, 250100, China.
authors.forename: He
authors.initials: H
authors.lastname: Hai-Lun
authors.forename: Chen
authors.initials: C
authors.lastname: Xiu-Lan
authors.forename: Sun
authors.initials: S
authors.lastname: Cai-Yun
authors.forename: Zhang
authors.initials: Z
authors.lastname: Yu-Zhong
authors.forename: Zhou
authors.initials: Z
authors.lastname: Bai-Cheng
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D000818:Animals; D033364:Decapoda / Q000737:chemistry*; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D007703:Peptidyl-Dipeptidase A; D012623:Seawater
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D010447:Peptide Hydrolases; D007703:Peptidyl-Dipeptidase A