大鳞副泥鳅蛋白ACE抑制肽的分离纯化与鉴定

Isolation,purification and identification of ACE inhibitory peptide from Paramisgurnus dabryanus protein

目的:开发大鳞副泥鳅的ACE抑制肽。方法:采用超滤、葡聚糖凝胶(Sephadex G-15)和半制备型高效液相色谱等多种技术,从大鳞副泥鳅蛋白酶解产物中分离纯化制备了高活性的ACE抑制肽,并利用高效液相色谱质谱—串联质谱对其结构进行解析;利用抑制动力学分析纯化后ACE抑制肽的抑制模式。结果:高活性ACE抑制肽的氨基酸序列为Glu-Gly-His,相对分子质量345.2 Da,IC50值为(17.89±3.28)μg/mL,纯化倍数为27.47。结论:大鳞副泥鳅抑制肽是一种竞争性的ACE抑制肽。

Objective:This study aimed to develop ACE inhibitory peptide of Paramisgurnus dabryanus.Methods:Ultrafiltration,Sephadex G-15 and RP-HPLC were used to isolate and purify ACE inhibitory peptides from the proteolysis products of P.dabryanus,and their structures were analyzed by HPLC-MS/MS.The inhibitory mode of purified ACE inhibitory peptide was analyzed by inhibition kinetics.Results:The amino acid sequence of ACE inhibitory peptide was Glu-Gly-HIS,the relative molecular weight was 341.2 Da,the IC50value was(17.89±3.28)μg/mL,and the purification ratio was 27.47.Conclusion:The inhibitory peptide of P.dabryanus is a competitive ACE inhibitory peptide.