NDLI: Isolation of a calcium-binding peptide from bovine serum protein hydrolysates

Content Provider	Springer Nature Link
Author	Choi, Dong Won Lee, Ji Hye Chun, Ho Hyun Song, Kyung Bin
Copyright Year	2012
Abstract	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.
Starting Page	1663
Ending Page	1667
Page Count	5
File Format	PDF
ISSN	12267708
Journal	Food Science and Biotechnology
Volume Number	21
Issue Number	6
e-ISSN	20926456
Language	English
Publisher	The Korean Society of Food Science and Technology
Publisher Date	2012-12-31
Publisher Place	Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	calcium binding peptide enzymatic hydrolysate isolation bovine serum protein Food Science Nutrition
Content Type	Text
Resource Type	Article
Subject	Applied Microbiology and Biotechnology Food Science Biotechnology

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