Extraction,Isolation and ACE inhibition of Peptides from Sturgeon (Acipenser schrenckii) Skin
[Objective]To determine the optimal enzymatic hydrolysis conditions and ACE inhibition for Acipenser schrenckii skin peptides (ASPs )and explore the feasibility of their application in the targeted development of angiotensin-converting enzyme (ACE) inhibitory active peptides[Method]The basic components of sturgeon skin were determined according to the national standard method.With the degree of hydrolysis and ACE inhibition as indices,the optimal enzymatic hydrolysis conditions of sturgeon skin peptide were determined by single factor experiment for the optimal hydrolase enzyme,enzyme dosage,solid-liquid ratio,temperature and time.Ultrafiltration membrane equipment with different relative molecular weight cut-offs was used to separate sturgeon skin peptides,and their ACE inhibition rates were compared.Subsequently,the optimal peptide components were studied by ultraviolet spectroscopy,relative molecular weight range determination,peptide sequence determination,and biological activity prediction.[Results and Conclusion]The dry base of sturgeon skin was mainly composed of protein and fat.The optimal enzymatic hydrolysis conditions of sturgeon skin peptide were alkaline protease,enzyme addition 6000 U/g,solid-liquid ratio 1:5 (g/mL),60 ℃,and 7 h.The relative molecular weight range of ASPs-1,the optimal peptide component,was 172.13-2135.02 u,and a total of 28 peptides with a comprehensive score greater than 100 were identified,with a relative molecular weight of 807.45-1952.96 u.Among them,GPGGPSGERGPPGPM,GPSGPGGPPGPR,SGPPGFPGSPGPKGE,GPPGKDGQPGHPGPIGPA,GPAGPA were predicted to have ACE inhibition function,and had good water solubility and no biological toxicity.Therefore,it is speculated that ASPs-1 has the potential to be used as an ACE inhibitor in living organisms.
Acipenser schrenckii skin peptidesenzymatic extractionisolation and purificationidentificationACE inhibitionbiological activity
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