Isolation And Purification Of Antihypertensive Peptides From Porcine Femoral Head Collagen
Keywords
Enzymatic Hydrolysis, Antihypertensive Peptide, Ultrafiltration, Ion Exchange Chromatography, Gel Chromatography, Angiotensin-Converting Enzyme Half Inhibitory Concentration
Abstract
Alkaline protease, papain and flavor protease were used in sequence to enzymatically hydrolyze pig femoral head collagen to prepare antihypertensive peptides. In order to obtain highly active and high-purity antihypertensive peptides, ultrafiltration, ion exchange chromatography, and gel chromatography were used to separate and purify the enzymatic hydrolyzate, and in vitro detection methods were used to determine the activity of each isolated product on angiotensin-converting enzyme. Half inhibitory concentration (IC50 value). The results show that: the pig bone enzymatic hydrolyzate was separated by ultrafiltration to obtain a component with a molecular mass of less than 5 ku, which has the highest inhibitory activity against angiotensin-converting enzyme, with an IC50 value of 1.400 2 mg/mL; this component was separated by ion exchange chromatography Four components were obtained, of which component 2 had the highest activity, with an IC50 value of 0.488 4 mg/mL; component 2 was then subjected to gel chromatography to separate four components, of which component 2-2 had the highest activity. IC50 value is 0.195 3 mg/mL
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Original research was done by Fu Gang, Liu Xiaohong, Li Cheng, Su Zhao
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