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KMID : 1007520120210061663
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Food Science and Biotechnology
2012 Volume.21 No. 6 p.1663 ~ p.1667
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Isolation of a Calcium-binding Peptide from Bovine Serum Protein Hydrolysates
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Choi Dong-Won
Lee Ji-Hye
Chun Ho-Hyun
Song Kyung-Bin
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Abstract
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A calcium-binding peptide was isolated from the hydrolysates of bovine serum protein (BSP). BSP was hydrolyzed using 3 different types of proteases, Alcalase, Flavourzyme, and Protamex, and the degree of hydrolysis was determined and monitored using trinitrobenzenesulfonic acid and SDS-PAGE. The hydrolysates of BSP using Alcalase were selected and ultra-filtered below 3 kDa. The membrane-filtered solution was then fractionated using ion exchange chromatography and normal phase HPLC to isolate a calcium-binding peptide. The calcium-binding capacity was determined by the orthophenanthroline method. The sequence of the purified calcium-binding peptide was analyzed using LC/electron spray ionization (LC/ESI)- tandem mass spectroscopy and identified to be Asp-Asn- Leu-Pro-Asn-Pro-Glu-Asp-Arg-Lys-Asn-Tyr-Glu, which has a molecular weight of 1,603 Da.
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KEYWORD
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calcium binding peptide, enzymatic hydrolysate, isolation, bovine serum protein
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