Purification and Identification of Antioxidant Peptides from Enzymatic Hydrolysate of Spirulina platensis

J Microbiol Biotechnol. 2016 Jul 28;26(7):1216-23. doi: 10.4014/jmb.1601.01033.

Abstract

The aim of this study was to isolate antioxidant peptides from an enzymatic hydrolysate of Spirulina platensis. A novel antioxidant peptide was obtained by ultrafiltration, gel filtration chromatography, and reverse-phase high-performance liquid chromatography, with the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay used to measure the antioxidant activity, and the sequence was determined to be Pro-Asn-Asn (343.15 Da) by electrospray ionization tandem mass spectrometry. This peptide was synthesized to confirm its antioxidant properties, and it exhibited 81.44 ± 0.43% DPPH scavenging activity at 100 µg/ml, which was similar to that of glutathione (82.63 ± 0.56%). Furthermore, the superoxide anion and hydroxyl free-radical scavenging activities and the SOD activity of the peptide were 47.84 ± 0.49%, 54.01 ± 0.82%, and 12.55 ± 0.75%, respectively, at 10 mg/ml. These results indicate that S. platensis is a good source of antioxidant peptides, and that its hydrolysate may have important applications in the pharmaceutical and food industries.

Keywords: Antioxidant peptide; Spirulina platensis; free-radical scavenging activity; mass spectrometry; purification.

MeSH terms

  • Antioxidants / chemistry*
  • Antioxidants / isolation & purification*
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Free Radical Scavengers
  • Glutathione
  • Hydrolysis
  • Oxidation-Reduction
  • Peptides / chemistry*
  • Peptides / isolation & purification*
  • Protein Hydrolysates / chemistry
  • Spirulina / chemistry*

Substances

  • Antioxidants
  • Free Radical Scavengers
  • Peptides
  • Protein Hydrolysates
  • Glutathione