Study On The Preparation Of Angiotensin-Converting Enzyme Inhibitory Peptide By Enzymatic Hydrolysis Of Collagen
Keywords
Angiotensin-Converting Enzyme, Inhibitory Peptide, Gel Filtration Chromatography, Reversed-Phase High Performance Liquid Chromatography, Hypertension
Abstract
? Angiotensin-converting enzyme (angiotensin-convertingenzyme, ace) inhibitors are currently important drugs used to treat hypertension. In this experiment, a combination of pepsin and trypsin was used to enzymatically hydrolyze collagen to prepare a hydrolyzate. The hydrolyzate was subjected to ultrafiltration using a 1kd ultrafiltration membrane, and the ultrafiltrate was subjected to dextran gel sephadexg-15 gel filtration chromatography to obtain various components. Each component was measured by enzyme activity and protein concentration, and two samples with higher ACE inhibition rate were screened out. Continue to use reversed-phase high-performance liquid chromatography to further separate and screen the samples. The protein concentration and inhibition rate of the different separated components are measured. By analyzing the experimental data, the components with the highest activity are screened out. The final sample was desalted and freeze-dried to determine the molecular weight of the angiotensin-converting enzyme inhibitory peptide with high inhibitory activity.
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Original research was done by Kong Qing, Li Jing, Bi Tao, Guan Bin, Chen Feng
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