Isolation and Identification of β-Casein A1-4P and β-Casein A2-4P in Commercial Casemates

Journal of Agricultural and Food Chemistry

Volumn 46, Issue 1, 1998, Pages 77-83

  Ward, Loren S ^a   Bastian, Eric D ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Caseinate; Dephosphorylation; Phosphatase; casein

Indexed keywords

EID: 0002640319     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9706585     Document Type: Article

References (29)

1. Andrews, A. T, Bovine milk acid phosphatase II. Binding to casein substrates and heat-inactivation studies. J. Dairy Res. 1974, 41, 229-237.
2. Andrews, A. T. Phosphatases in milk. In Advanced Dairy Chemistry, Vol. 1-Proteins; Fox, P. F., Ed.; Elsevier Science Publishers: London, 1992; pp 322-331.
3. Andrews, A. T.; Pallavicini, C. Bovine milk acid phosphatase I. Some kinetic studies and other properties using a partially purified preparation. Biochim. Biophys. Acta 1973, 321, 197-209.
4. Bovenhuis, H.; Verstege, A. J. M. Improved method for phenotyping milk protein variants by isoelectric focusing using PhastSystem. Neth. Milk Dairy J. 1989, 43, 447-451.
5. Creamer, L. K.; Matheson, A. R. Action of alkali on casein. N. Z. J. Dairy Sci. Technol. 1977, 12, 253-259.
6. Davies, D. T.; Law, A. J. R. Quantitative fractionation of casein mixtures by fast protein liquid chromatography. J. Dairy Res. 1987, 54, 369-376.
7. de Koning, P. J.; van Rooijen, P. J. Aspects of the formation of lysinoalanine in milk and milk products. J. Dairy Res. 1982, 49, 725-736.
8. Eigel, W. N.; Butler, J. E.; Ernstrom, C. A.; Farrell, H. M., Jr.; Harwalkar, V. R.; Jenness, R.; Whitney, R. McL. Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci. 1984, 67, 1599-1631.
9. Friedman, M.; Zahnley, J. C.; Masters, P. M. Relationship between in vitro digestibility of casein and its content of lysinoalanine and D-amino acids. J. Food Sci. 1981, 46, 127-131.
10. Haab, W.; Smith, L. M. Variations in alkaline phosphatase activity of milk. J. Dairy Sci. 1956, 39, 1644-1650.
11. s1- and β-caseins by alkali treatment. Agric. Biol. Chem. 1981, 45, 1645-1651.
12. Hollar, C. M. Phenotyping milk protein variants with isoelectric focusing using PhastSystem®. In Estimation of selected milk protein genetic variants by multicomponent analysis of amino acid profiles. Ph.D. Dissertation, Utah State University, 1992.
13. 31P-NMR studies of bovine β-casein. Biochim. Biophys. Acta 1982, 708, 294-299.
14. Jenness, R.; Patton, S. Milk enzymes. In Principles of Dairy Chemistry; Wiley: New York, 1959; pp 182-203.
15. Kitchen, B. J. Indigenous milk enzymes. In Developments in Dairy Chemistry; Fox, P. F., Ed.; Elsevier Applied Science: London, 1985; pp 239-279.
16. Lorient, D. Covalent bonds formed in proteins during milk sterilization: studies on caseins and casein peptidee. J. Dairy Res. 1979, 46, 393-396.
17. Lorient, D.; Linden, G. Dephosphorylation of bovine casein by milk alkaline phosphatase. J. Dairy Res. 1976, 43, 19-26.
18. Manson, W. The lability of the phosphate groups of β-casein towards alkali. Neth. Milk Dairy J. 1973, 27, 181-187.
19. Manson, W.; Carolan, T. Formation of lysinoalanine from individual bovine caseins. J. Dairy Res. 1980, 47, 193-198.
20. Mulvihill, D. M. Production, functional properties and utilization of milk protein products. In Advanced Dairy Chemistry, Vol. 1-Proteins; Fox, P. F., Ed.; Elsevier Science Publishers: London, 1992; pp 369-404.
21. Parker, T. G.; Dalgleish, D. G. Binding of calcium ions to bovine β-casein. J. Dairy Res. 1981, 48, 71-76.
22. Sternberg, M.; Kim, C. Y. Lysinoalanine formation in protein food ingredients. In Protein Crosslinking: Nutritional and Medical Consequences; Mendel, F., Ed.; Plenum Press: New York, 1977; pp 73-84.
23. Swaisgood, H. E. Chemistry of the caseins. In Advanced Dairy Chemistry, Vol. 1-Proteins; Fox, P. F., Ed.; Elsevier Science Publishers: London, 1992; pp 63-109.
24. Ward, L. S.; Bastian, E. D. A method for isolating β-casein. J. Dairy Sci. 1996, 79, 1332-1339.
25. West, D. W. Structure and function of the phosphorylated residues of casein. J. Dairy Res. 1986, 53, 333-352.
26. West, D. W.; Dalgleish, D. G. A kinetic analysis of the dephosphorylation, by bovine spleen phosphoprotein phosphatase (EC 3.1.3.16) of a phosphopeptide derived from β-casein. Biochim. Biophys. Acta 1976, 438, 169-175.
27. Yoshikawa, M.; Tamaki, M.; Sugimoto, E.; Chiba, H. Effect of dephosphorylation on the self-association and the precipitation of β-casein. Agric. Biol. Chem. 1974, 38, 2051-2052.
28. Yun, S.; Ohmiya, K.; Shimizu, S. Role of the phosphoryl group of β-casein in milk curdling. Agric. Biol. Chem. 1982, 46, 1505-1511.
29. Zittle, C. A.; Bingham, E. W. Action of purified milk phosphatase on phosphoserine and on casein. J. Dairy Sci. 1959, 42, 1772-1780.