Deamidation kinetics of casein precipitated by carbon dioxide compared with commercial caseinates

Journal of Food Science

Volumn 64, Issue 3, 1999, Pages 400-404

  Santos, C V ^a   Tomasula, P M ^a   Kurantz, M J ^a  

^a EASTERN REGIONAL RESEARCH CENTER   (United States)

Author keywords

Amides; Carbon dioxide; Casein; Deamidation; Kinetics

Indexed keywords

ARRHENIUS;

EID: 0033057272     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1999.tb15051.x     Document Type: Article

References (31)

1. Casella, M.L.A. and Whitaker, J.R. 1990. Enzymatically and chemically modified zein for improvement of functional properties. J. Food Biochem. 14: 453-475.
2. Claughton, S.M. and Pearce, R.J. 1989. Preparation and properties of acid-modified sunflower protein isolate. J. Food Sci. 54: 357-361.
3. Eigel, W.N., Butler, J.E., Ernstrom, C.A., Farrell Jr., H.M., Harwalkar, V.R., Jenness, R., and Whitney, R. 1984. Nomenclature of proteins of cow's milk: Fifth revision. J. Dairy Sci. 67: 1599-1631.
4. Friedl, G.L. and Howell, N. 1996. Gelation properties of deamidated soluble wheat proteins. Food Hydrocolloids 10: 255-261.
5. Geiger, T. and Clarke, S. 1987. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. J. Biol. Chem. 262: 785-794.
6. Hamada, J.S. 1992. Effects of heat and proteolysis on deamidation of food proteins using peptidoglutaminase. J. Agric. Food Chem. 40: 719-723.
7. Hamada, J.S. and Marshall, J. 1992. Effect of heat and proteolysis on deamidation of food proteins using peptidoglutaminase. J. Agric. Food Chem. 40: 719-723
8. Kinsella, J.E., 1984. Milk Proteins: Physicochemical and functional properties. CRC Crit. Rev. Food. Sci. Nutr. 21: 197-262.
9. Ma, C.-Y. and Khanzada, G. 1987. Functional properties of deamidated oat protein isolates. J. Food Sci. 52: 1583-1587.
10. Matsudomi, N., Sasaki, T., Kato, A., and Kobayashi, K. 1985. Conformational changes and functional properties of acid-modified soy protein. Agric. Biol. Chem. 49: 1251-1256.
11. Metwalli, A. A.M. and van Boekel, M.A.J.S. 1998. On the kinetics of heat-induced deamidation and breakdown of caseinate. Food Chem. 61: 53-61.
12. Mine, Y. 1997. Effect of dry heat and mild alkaline treatment on functional properties of egg white proteins. J. Agric. Food Chem. 45: 2924-2928.
13. g1-casein by transglutaminase. Agric. Biol. Chem. 50: 3025-3030.
14. Robinson, A.B., Scotchler, J.W., and McKerrow, J.H. 1973. Raies of nonenzymatic deamidation of glutaminyl and asparaginyl residues in pentapeptides. J. Am. Chem. Soc. 95: 8156-8159.
15. Roeper, J., Preparation of calcium casemate from casein curd. 1977. N.Z. Dairy J. Dairy Sci. Technol. 12: 182-189.
16. Shih, F.F. 1990. Deamidation during treatment of soy protein. J. Food Sci. 55: 127-129.
17. Shih, F. F. 1991. Effect of anions on the deamidation of soy protein. J. Food Sci. 56: 452-454.
18. Shih, F.F. 1992. Modification of food proteins by non-enzymatic methods. Ch. 7 in Biochemistry of Food Proteins. B.J.F. Hudson (Ed.). p.235-248. Elsevier Science Publishers Ltd., New York.
19. Scotchler, J.W. and Robinson, A.B. 1974. Deamidation of glutaminyl residues: dependence on pH, temperature, and ionic strength. Analytical Biochemistry 59: 319-322.
20. Snedecor, G. W. and Cochran, W.G. 1989. Statistical Methods, 8th ed. Iowa State University Press, Ames, IA.
21. Sohn, M. and Ho C.-T. 1995. Ammonia generation during thermal degradation of amino acids. J. Agric. Food Chem. 43: 3001-3003.
22. Stephenson, R.C. and Clarke, S. 1989. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 264: 6164-6170.
23. Swaisgood, H.E. 1992. Chemistry of the caseins. Ch. 2 in Advanced Dairy Chemistry-Volume I: Proteins, PF. Fox (Ed.), p.82. Elsevier Science Publishers Ltd., New York
24. Tomasula P.M., Craig Jr., J.C., Boswell, R.T., Cook, R.D., Kurantz, M.J., and Maxwell, M. 1995. Preparation of casein using carbon dioxide. J. Dairy Sci. 78: 506-514.
25. Tyler-Cross, R. and Schirch, V. 1991. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J. Biol. Chem. 33: 22549-22556.
26. Wagner, J.R. and Guegen, J. 1995. Effects of dissociation, deamidation, and reducing treatment on structural and surface-active properties of soy glycinin. J. Agric. Food Chem. 43: 1993-2000.
27. Wright, H.T. 1991a. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol. 26: 1-52.
28. Wright, H.T. 1991b. Sequence and structure determinants of the nonenzymatic deamidation of asparagine and glutamine residues in proteins. Prot. Engr. 4: 283-294.
29. Zhang, J., Lee, T.C., and Ho, C.-T. 1993a. Comparative study on kinetics of nonenzymatic deamidation of soy protein and egg white lysozyme. J. Agric Food Chem. 41: 2286-2290.
30. Zhang, J., Lee, T.C., and Ho, C.-T. 1993b. Kinetics and mechanism of nonenzymatic deamidation of soy protein. J. Food Processing and Preserv. 17: 259-268.
31. Zhang, J., Lee, T.C., and Ho, C.-T. 1993c. Thermal deamidation of proteins in a restricted water environment. J. Agric. Food Chem. 41: 1840-1843.