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Isolation of a Calcium-binding Peptide from Chlorella Protein Hydrolysates

  • Jeon, So-Jeong (Department of Food Science and Technology, Chungnam National University) ;
  • Lee, Ji-Hye (Department of Food Science and Technology, Chungnam National University) ;
  • Song, Kyung-Bin (Department of Food Science and Technology, Chungnam National University)
  • Received : 2010.10.08
  • Accepted : 2010.11.26
  • Published : 2010.12.31

Abstract

To isolate a calcium-binding peptide from chlorella protein hydrolysates, chlorella protein was extracted and hydrolyzed using Flavourzyme, a commercial protease. The degree of hydrolysis and calcium-binding capacity were determined using trinitrobenzenesulfonic acid and orthophenanthroline methods, respectively. The enzymatic hydrolysis of chlorella protein for 6 hr was sufficient for the preparation of chlorella protein hydrolysates. The hydrolysates of chlorella protein were then ultra-filtered under 5 kDa as molecular weight. The membrane-filtered solution was fractionated using ion exchange, reverse phase, normal phase chromatography, and fast protein liquid chromatography to identify a calcium-binding peptide. The purified calcium-binding peptide had a calcium binding activity of 0.166 mM and was determined to be 700.48 Da as molecular weight, and partially identified as a peptide containing Asn-Ser-Gly-Cys based on liquid chromatography/electrospray ionization tandem mass spectrum.

Keywords

References

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