Molecules (May 2019)

Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein

  • Xueqin Wang,
  • Huahua Yu,
  • Ronge Xing,
  • Song Liu,
  • Xiaolin Chen,
  • Pengcheng Li

DOI
https://doi.org/10.3390/molecules24101946
Journal volume & issue
Vol. 24, no. 10
p. 1946

Abstract

Read online

The aim of this study was to isolate and purify antioxidative peptides from Pacific herring (Clupea pallasii) protein. Five enzymes (pepsin, trypsin, papain, flavourzyme, and neutrase) were used for protein hydrolysis, and Pacific herring protein hydrolysates (PHPH) were separated by ultrafiltration. The fraction with the molecular weight below 3500 Da exhibited the highest in vitro antioxidant activities and cellular antioxidant activity. The PHPH was isolated and purified by consecutive chromatographic methods including gel filtration chromatography and reverse high-performance liquid chromatography (RP-HPLC). The purified antioxidant peptides were identified as Leu-His-Asp-Glu-Leu-Thr (MW = 726.35 Da) and Lys-Glu-Glu-Lys-Phe-Glu (MW = 808.40 Da), and the IC50 values of cellular antioxidant activity were 1.19 ± 0.05 mg/mL and 1.04 ± 0.06 mg/mL. The results demonstrate that is possible to produce natural antioxidative peptides from Pacific herring protein via enzymatic hydrolysis and purification.

Keywords