Characterization of Salt-Soluble Protein from Mytilus edulis and Enzymatic Preparation of ACE Inhibitory Peptides

doi:10.7506/spkx1002-6630-201822009

Abstract

Abstract: The molecular mass distribution, particle size distribution and degeneration temperature of the salt-soluble protein from Mytilus edulis muscle were studied. The tryptic hydrolysate of M. edulis muscle was found to have higher angiotensin converting enzyme (ACE) inhibitory activity than the hydrolysates produced with neutral protease and pancreatin, with a half maximal inhibitory concentration (IC50) of 215.96 μg/mL. The amino acid sequences of peptides from the tryptic hydrolysate were identified by mass spectrometry. Eleven peptides bound to ACE with scores greater than 180 were selected. The interaction and hydrogen bonds between amino acid binding sites were analyzed to screen active peptides and the mechanism of antihypertensive activity was elucidated. Finally, LYDIDVAK and WIAEEADK were predicted as peptides with high ACE inhibitory activity.

Key words: Mytilus edulis, salt-soluble protein, ultra performance liquid chromatography quadrupole time of flight (UPLC-Q-TOF), angiotensin converting enzyme (ACE) inhibitory peptide, molecular docking

CLC Number:

TS254

QIAO Meiling, LIU Hanxiong, FAN Fengjiao, TU Maolin, YU Cuiping, DU Ming. Characterization of Salt-Soluble Protein from Mytilus edulis and Enzymatic Preparation of ACE Inhibitory Peptides[J]. FOOD SCIENCE, 2018, 39(22): 51-56.

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Characterization of Salt-Soluble Protein from Mytilus edulis and Enzymatic Preparation of ACE Inhibitory Peptides

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