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

Abstract

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 IC50 value 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.

Keywords

• paramisgurnus dabryanus
• ace inhibitory peptide
• isolation and purification
• structure identification
• inhibition