Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry

Jiaoyan Ren; Mouming Zhao; John Shi; Jinshui Wang; Yueming Jiang; Chun Cui; Yukio Kakuda; Sophia Jun Xue

doi:10.1016/j.foodchem.2007.11.010

Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry

Food Chem. 2008 May 15;108(2):727-36. doi: 10.1016/j.foodchem.2007.11.010. Epub 2007 Nov 17.

Authors

Jiaoyan Ren¹, Mouming Zhao², John Shi³, Jinshui Wang¹, Yueming Jiang⁴, Chun Cui¹, Yukio Kakuda⁵, Sophia Jun Xue³

Affiliations

¹ College of Light Industry and Food Science, South China University of Technology, Guangzhou 510640, China.
² College of Light Industry and Food Science, South China University of Technology, Guangzhou 510640, China. Electronic address: femmzhao@scut.edu.cn.
³ Guelph Food Research Center, Agriculture and Agri-Food Canada, Guelph, Ontario, Canada N1G 5C9.
⁴ South China Botanical Garden, The Chinese Academy of Sciences, Guangzhou, Leyiju 510650, China.
⁵ Department of Food Science, University of Guelph, Guelph, Ontario, Canada N1G 2W1.

PMID: 26059154
DOI: 10.1016/j.foodchem.2007.11.010

Abstract

Grass carp muscles were hydrolyzed with various proteases (papain, bovine pancreatin 6.0, bromelain, neutrase 1.5MG and alcalase 2.4L) to extract antioxidant peptides. The hydrolysates were assessed using methods of hydroxyl radical scavenging ability and lipid peroxidation inhibition activity. Hydrolysate prepared with alcalase 2.4L was found to have the highest antioxidant activity. It was purified using ultrafiltration and consecutive chromatographic methods including ion-exchange chromatography, multilayer coil high-speed counter-current chromatography, and gel filtration chromatography. The purified peptide, as a potent antioxidant, was identified as Pro-Ser-Lys-Tyr-Glu-Pro-Phe-Val (966.3Da) using RP-HPLC connected on-line to an electrospray ionization mass spectrometry. As well, it was found that basic peptides had greater capacity to scavenge hydroxyl radical than acidic or neutral peptides and that hydrophobic peptides contributed more to the antioxidant activities of hydrolysates than the hydrophilic peptides. In addition, the amino acid sequence of the peptide might play an important role on its antioxidant activity.

Keywords: Antioxidant peptides; Electrospray ionization-mass spectrometry; Grass carp muscle; High-speed counter-current chromatography.