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Article isolation of a calcium-binding peptide from enzymatic hydrolysates of porcine blood plasma protein

Authors
  • Lee, Seung Hwan1
  • Song, Kyung Bin1
  • 1 Chungnam National University, Department of Food Science and Technology, Daejeon, 305-764, Republic of Korea , Daejeon
Type
Published Article
Journal
Journal of the Korean Society for Applied Biological Chemistry
Publisher
Springer-Verlag
Publication Date
Jun 01, 2009
Volume
52
Issue
3
Pages
290–294
Identifiers
DOI: 10.3839/jksabc.2009.051
Source
Springer Nature
Keywords
License
Yellow

Abstract

A calcium-binding peptide was purified from hydrolysates of porcine plasma protein. Porcine plasma protein was hydrolyzed using Flavourzyme, and the hydrolysates were filtered using YM-3 membrane. The membrane filtered solution was fractionated using Sephadex G-15, normal phase high-performance liquid, ion exchange chromatography, and fast protein liquid chromatography for a calcium-binding peptide. The sequence of the purified calcium-binding peptide was analyzed using liquid chromatography/electron spray ionization tandem mass spectrum and identified to be Val-Ser-Gly-Val-Glu-Asp-Val-Asn. The calcium- binding peptide can be used as a food ingredient or feed for calcium deficiency.

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