Preparation of Angiotensin-converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Collagen

Abstract

Abstract: Angiotensin-converting enzyme(ACE) inhibitors are very important drugs for clinical treatment of hypertension.Pepsin and trypsin were used together to prepare the hydrolysates from collagen.Ultrafiltrations(UF) with 1 kD membrane and gel filtration chromatography(GFC) with Sephadex G-15 were used to separate the hydrolysates into different components.By measuring the inhibitory activity and protein concentration of the components,two samples with the greatest inhibitory activity were selected.The samples were then taken to further separate by reverse phase high performance liquid chromatography(RP-HPLC).Different components of the samples were collected.The same methods as that mentioned above were taken to screen the optimum component.After desalting and freezing drying,the molecular mass of component with the greatest inhibitory activity was determined at last.

Key words: angiotensin-converting enzyme, inhibitory peptides, gel filtration chromatography, reverse phase high performance liquid chromatography, hypertension

KONG Qing, LI Jing, BI Tao, GUAN Bin, CHEN Feng. Preparation of Angiotensin-converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Collagen[J]. FOOD SCIENCE, 2008, 29(5): 298-302.

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Preparation of Angiotensin-converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Collagen

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