Heat-induced deamidation, dephosphorylation and breakdown of caseinate

International Dairy Journal

Volumn 9, Issue 3-6, 1999, Pages 237-241

  Van Boekel, Martinus A J S ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Casein; Deamidation; Dephosphorylation; Heat induced proteolysis; Kinetics

Indexed keywords

ASPARAGINE; BETA CASEIN; CASEINATE; DEAMINATION; DEHYDROALANINE; DEPHOSPHORYLATION; HEAT; LYSINOALANINE; NITROGEN; PHOSPHATE; PROTEIN HYDROLYSIS; SOLUTE CONCENTRATION; TEMPERATURE;

EID: 0032839314     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(99)00068-0     Document Type: Conference Paper

References (18)

1. Atkins P.W. Physical chemistry. 3rd ed:1986;Oxford University Press, Oxford.
2. Belec J., Jenness R. Dephosphorization of caseins by heat treatment. I. In caseinate solutions. Journal of Dairy Science. 45:1962;12-19.
3. π -(2′-amino-2′-carboxyethyl)-L-histidine ('histidinoalanine', HAL) in heated milk products Zeitschrift für Lebensmittel - Untersuchung und Forschung. 197:1993;114-117.
4. FIL.IDF. (1962). Determination of nitrogen content. FIL.IDF Standard 20.
5. FIL.IDF. (1990). Determination of total phosphorus content. FIL.IDF Standard 42B.
6. Jenness R., Koops J. Preparation and properties of a salt solution which simulates milk ultrafiltrate. Netherlands Milk and Dairy Journal. 16:1962;153-164.
7. Kleyn D.H., Klostermeyer H. Dehydroalanin als Reaktionsprodukt bei der Erhitzung von. β -casein Zeitschrift für Lebensmittel- Untersuchung und- Forschung. 170:1980;11-13.
8. Meisel H., Schlimme E. Casein-gebundener Phosphor und der Gehalt an freien Aminosäuren in unterschiedlich wärmebehandelter Milch. Kieler Milchwirtschaftliche Forschungsberichte. 47:1995;289-295.
9. Metwalli A.A.M., Metwalli N.H., Van Boekel M.A.J.S. Effect of urea on heat-induced changes in milk. Netherlands Milk Dairy Journal. 50:1996;427-457.
10. Meyer M., Klostermeyer H., Kleyn D.H. Verminderte Bildung von Lysinoalanin bei enzymatisch dephosphoryliertem Casein. Zeitschrift für Lebensmittel- Untersuchung und- Forschung. 172:1981;446-448.
11. Patel K., Borchardt R.T. Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharmaceutical Research. 7:1990;703-711.
12. Saidi B., Warthesen J.J. Heat and fermentation effects on total nonprotein nitrogen and urea in milk. Journal of Food Science. 58:1993;548-551.
13. Van Boekel M.A.J.S., Walstra P. Use of kinetics in studying heat-induced changes in foods. Fox P.F. Heat-induced changes in milk. 1995;22-50 International Dairy Federation, Brussels.
14. Walstra P., Jenness R. Dairy Chemistry & Physics. 1984;Wiley, New York.
15. Wright H.T. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Critical Reviews in Biochemistry and Molecular Biology. 26:1991;1-52.
16. Zhang J., Lee T.C., Ho Ch-T. Comparative study on kinetics of nonenzymatic deamidation of soy protein and egg white lysozyme. Journal of Agricultural and Food Chemistry. 41:1993;2286-2290.
17. Zhang J., Lee T.C., Ho Ch-T. Kinetics and mechanism of nonenzymatic deamidation of soy protein. Journal of Food Processing and Preservation. 17:1993;259-268.
18. Zhang J., Lee T.C., Ho Ch-T. Thermal deamidation of proteins in a restricted water environment. Journal of Agricultural and Food Chemistry. 41:1993;1840-1843.