Functional Properties of Dephosphorylated Bovine Whole Casein
β Scribed by Van Hekken, D.L.; Strange, E.D.
- Book ID
- 122141313
- Publisher
- American Dairy Science Association
- Year
- 1993
- Tongue
- English
- Weight
- 547 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0022-0302
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
phorylated, according to the specifications of the supplier The functional and interfacial properties of b-casein and de- (Sigma Chemical Co.). This results in the net negative phosphorylated b-casein (DeP b-casein) were studied at pH 7.0 charge of the N-terminal 50 amino acids, at pH 7.0, decreasin
exchange chromatography. Dephosphorylation of CPP was achieved using immobilized alkaline phosphatase. The purified phosphopeptides and their dephosphorylated forms obtained by these methods are suitable for comparative studies on biological activities, especially mineral binding and immunmodulation