Effect of Temperature, Feed Moisture, and pH on Protein Deamidation in an Extruded Wheat Flour

Journal of Agricultural and Food Chemistry

Volumn 41, Issue 2, 1993, Pages 199-202

  Izzo, Henry V ^a   Lincoln, Michelle D ^a   Ho, Chi Tang ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0008386624     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf00026a010     Document Type: Article

References (32)

1. AOAC. Official Methods of Analysis, 14th ed.; Association of Official Analytical Chemists: Washington, DC, 1986.
2. Aswad, D. W. Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. J. Biol. Chem. 1984, 259, 10714–10721.
3. Beutler, H. Ammonia. In Methods in Enzymatic Analysis, 3rd ed.; Academic Press: New York, 1984; Vol. 6, pp 639–645.
4. Bollecker, S.; Viroben, G.; Popineau, Y.; Gueguen, J. Acid deamidation and enzymic modification at pH 10 of wheat gliadins: influence on their functional properties. Sci. Aliments 1990, 10, 343–356.
5. Finley, J. W. Deamidated gluten: A potential fortifier for fruit juices. J. Food Sci. 1975, 40, 1283–1285.
6. Hamada, J. S. Effects of Heat and Proteolysis on Deamidation of Food Proteins Using Peptidoglutaminase. J. Agric. Food Chem. 1992, 40, 719–723.
7. Hamada, J. S.; Marshall, W. E. Preparation and functional properties of enzymatically deamidated soy proteins. J. Food Sci. 1989, 54, 598–601.
8. Izzo, H. V.; Ho, C.-T. Ammonia Affects Maillard Chemistry of an Extruded Autolyzed Yeast Extract: Pyrazine Aroma Generation and Brown Color Formation. J. Food Sci. 1992, 57, 657–659.
9. Izzo, M. T. Lipid-Protein and Lipid-Carbohydrate Interactions During Twin Screw Extrusion of Corn Meal. Ph.D. Dissertation, Rutgers University, 1989.
10. Johnson, B. A.; Aswad, D. W. Enzymatic protein carboxyl methylation at physiological pH: cyclic imide formation explains rapid methyl turnover. Biochemistry 1985, 24, 2581–2586.
11. Johnson, B. A.; Murray, D. E.; Clarke, S.; Glass, D. B.; Aswad, D. W. Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides. J. Biol. Chem. 1987, 262, 5622–5629.
12. Kato, A.; Tanaka, A.; Lee, Y.; Matsudomi, N.; Kobayashi, K. Effects of deamidation with chymotrypsin at pH 10 on the functional properties of proteins. J. Agric. Food Chem. 1987, 35, 285–288.
13. Kun, E.; Kearney, E. B. Ammonia. In Methods of Enzymatic Analysis, 2nd ed.; Bergmeyer, H. U., Ed.; Academic Press: New York, 1974; Vol. 4, pp 1802–1806.
14. Lowenson, J.; Clarke, S. Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? Blood Cells 1988, 14, 103–117.
15. Ma, C. Y.; Oomah, D.; Holme, J. Effect of deamidation and succinylation on some physico-chemical and baking properties of gluten. J. Food Sci. 1986, 51, 99–103.
16. Matsudomi, N.; Kaneko, S.; Kato, A.; Kobayashi, K. Functional properties of deamidated gluten. Nippon Nogeikagu Kaishi 1981, 55, 983–989.
17. Matsudomi, N.; Kato, A.; Kobayashi, K. Conformation and surface properties of deamidated gluten. Agric. Biol. Chem. 1982, 46, 1583–1586.
18. Matsudomi, N.; Sasaki, T.; Kato, A.; Kobayashi, K. Conformational changes and Functional properties of acid-modififed soy protein. Agric. Biol. Chem. 1985, 49, 1251–1256.
19. Murray, D. E.; Clarke, S. Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase. J. Biol. Chem. 1984, 259, 10722–10732.
20. Pomeranz, Y. Composition and functionality of wheat flour components. In Wheat Chemistry and Technology, 3rd ed.; Pomeranz, Y., Ed.; AACC: St. Paul, MN, 1988; Vol. 2, pp 242–284.
21. Popineau, Y.; Thebaudin, J. Y. Functional properties of enzymatically hydrolyzed glutens. In Gluten Proteins 1990; Bushuk, W., Tkachuk, R., Eds.; AACC: St. Paul, MN, 1991; pp 284–287.
22. Robinson, A. B.; Rudd, C. J. Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. Curr. Top. Cell. Regul. 1974, 8, 247–295.
23. Scotchler, J. W.; Robinson, A. B. Deamidation of glutaminyl residues: dependence on pH, temperature, and ionic strength. Anal. Biochem. 1974, 59, 319–322.
24. Shih, F. F. Deamidation of protein in soy extract by ion exchange resin catalysis. J. Food Sci. 1987, 52, 1529–1531.
25. Shih, F. F. Deamidation during treatment of soy protein with protease. J. Food Sci. 1990, 55, 127–129.
26. Shih, F. F. Effect of anions on the deamidation of soy protein. J. Food Sci. 1991, 56, 452–454.
27. Shih, F. F.; Kalmar, A. D. SDS-catalyzed deamidation of soy proteins. J. Agric. Food Chem. 1987, 35, 672–675.
28. Stephenson, R. C.; Clarke, S. Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 1989, 264, 6164–6170.
29. Wen, L. F.; Rodis, P.; Wasserman, B. P. Starch Fragmentation and Protein Insolubilization During Twin Screw Extrusion of Corn Meal. Cereal Chem. 1990, 67, 268–275.
30. Whitaker, J. R. Enzymatic Modification of Proteins Applicable to Foods. In Food Protein Improvement Through Chemical and Enzymatic Modification; Feeney, R. E., Whitaker, J. R., Eds.; American Chemical Society: Washington, DC, 1977; pp 95–96.
31. Wright T. H. Nonenzymatic deamidation of asparagynl and glutamyl residues in proteins. CRC Crit. Rev. Biochem. Mol. Biol. 1991, 26, 1–52.
32. Wu, C. H.; Shuryo, N.; Powrie, W. D. Preparation and properties of acid solubilized gluten. J. Agric. Food Chem. 1976, 24, 504–510.