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Isolation, Purification and Structural Analysis of ACE Inhibitory Peptides Derived from Red Pine (Pinus koraiensis Sieb. et Zucc.) Nuts Albumin

MIAO Xinyu, WANG Zuhao, WANG Peng, FANG Li, WANG Ji, MIN Weihong*   

  1. National Engineering Laboratory on Wheat and Corn Further Processing, College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China
  • Online:2017-03-15 Published:2017-03-28

Abstract: In this study, the composition and structural characteristics of angiotensin converting enzyme (ACE) inhibitory peptides derived from albumin extracted from red pine nuts were evaluated. The hydrolysate of albumin was separated by ultrafiltration, Sephadex G-25, Sephadex G-15 and reversed-phase high-performance liquid chromatography (RPHPLC). The structural characteristics of the purified fraction (D2) were identified by electrospray ionization tandem mass spectrometry (ESI-MS/MS), and one ACE inhibitory peptide was obtained with amino acid sequence of Tyr-Leu-Leu-Lys (YLLK) and molecular mass of 535.34 D. According to the amino acid sequence, an ACE inhibitory peptide was synthesized with a purity of 99.8%. The half maximal inhibitory concentration value of YLLK was 0.282 5 μmol/L.

Key words: red pine nut albumin, ACE inhibitory peptide, isolation and purification, amino acid sequence

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