Nonenzymatic Deamidation of Food Proteins

Critical Reviews in Food Science and Nutrition

Volumn 36, Issue 3, 1996, Pages 225-255

  Riha III, William E ^a   Izzo, Henry V ^a   Zhang, Jie ^a   Ho, Chi Tang ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

Ammonia; Deamidation; Protein

Indexed keywords

TRITICUM AESTIVUM; ZEA MAYS;

AMIDE; AMMONIA; ASPARAGINE; GLUTAMINE; VEGETABLE PROTEIN;

CHEMISTRY; FOOD; FOOD HANDLING; GLYCATION; PH; PLANT; REVIEW;

AMIDES; AMMONIA; ASPARAGINE; FOOD; FOOD HANDLING; GLUTAMINE; HYDROGEN-ION CONCENTRATION; MAILLARD REACTION; PLANT PROTEINS; PLANTS, EDIBLE;

EID: 0030079437     PISSN: 10408398     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408399609527724     Document Type: Article

References (102)

1. Robinson, A. B. and Rudd, C. J., Deamidation of glutaminyl and asparaginyl residues in peptides and proteins, Curr. Tip. Cell. Regul., 8, 247, 1974.
2. Wright, H. T., Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins, Crit. Rev. Biochem. Mol. Biol., 26, 1, 1991.
3. Whitaker, J. R., Enzymatic modification of proteins applicable to foods, in Food Protein Improvement Through Chemical and Enzymatic Modification, Feeney, R. E. and Whitaker, J. R., Eds., American Chemical Society, Washington, D.C., 95, 1977.
4. Matsudomi, N., Sasaki, T., Kato, A., and Kobayashi, K., Conformational changes and functional properties of acid-modified soy protein, Agric. Biol. Chem., 49, 1251, 1985.
5. Hamada, J. S. and Marshall, W. E., Preparation and functional properties of enzymatically deamidated soy proteins, J Food Sci., 54, 598, 1989.
6. Finley, J. W., Deamidated gluten: a potential fortifier for fruit juices, J. Food Sci., 40, 1283, 1975.
7. Izzo, H. V., Lincoln, M. D., and Ho, C.-T., Effect of temperature, feed moisture, and pH on protein deamidation in an extruded wheat flour, J. Agric. Food Chem., 41, 199, 1993.
8. Wu, C. H., Nakai, S., and Powrie, W. D., Preparation and properties of acid solubilized gluten, J. Agric. Food Chem., 24, 504, 1976.
9. Matsudomi, N., Kaneko, S., Kato, A., and Kobayashi, K., Functional properties of deamidated gluten, Nippon Nogeikagu Kaishi., 55, 983, 1981.
10. Matsudomi, N., Kato, A., and Kobayashi, K., Conformation and surface properties of deamidated gluten, Agric. Biol. Chem., 46, 1583, 1982.
11. Ma, C. Y., Oomah, D., and Holme, J., Effect of deamidation and succinylation on some physico-chemical and baking properties of gluten, J. Food Sci., 51, 99, 1986.
12. Shih, F. F., Effect of anions on the deamidation of soy protein, J. Food Sci., 56, 452, 1991.
13. Bollecker, S., Viroben, G., Popineau, Y., and Gueguen, J., Acid deamidation and enzymatic modification at pH 10 of wheat gliadins: influence on their functional properties, Sciences Aliments, 10, 343, 1990.
14. Popineau, Y. and Thebaudin, J. Y., Functional properties of enzymatically hydrolyzed glutens, in Gluten Proteins 1990, Bushuk, W. and Tkachuk, R., Eds., American Association of Cereal Chemists, St. Paul, MN, 1991, 287.
15. Kato, A., Tanaka, A., Lee, Y., Matsudomi, N., and Kobayashi, K., Effects of deamidation with chymotrypsin at pH 10 on the functional properties of proteins, J. Agric. Food Chem., 35, 285, 1987.
16. Shih, F. F., Deamidation during treatment of soy protein with protease, J. Food Sci., 55, 127, 1990.
17. Bollecker, S. and Popineau, Y., Functional properties of deamidated gliadins, in Gluten Proteins, 29, 1992.
18. Beckwith, A. C., Wall, J. S., and Dimler, R. J., Amide groups as interaction sites in wheat gluten proteins: effect of amide-ester conversion, Arch. Biochem. Biophys., 103, 319, 1963.
19. Krull, L. H. and Wall, J. S., Synthetic polypeptides containing side chain amide groups. Water-soluble polymers, Biochemistry, 5, 1521, 1966.
20. Aswad, D. W., Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25, J. Biol. Chem., 259, 10714, 1984.
21. Murray, D. E. and Clarke, S., Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase, J Biol. Chem., 259, 10722, 1984.
22. Johnson, B. A. and Aswad, D. W., Enzymatic protein carboxyl methylation at physiological pH; cyclic imide formation explains rapid methyl turnover, Biochemistry, 24, 2581, 1985.
23. Johnson, B. A., Murray, D. E., Clarke, S., Glass, D. B., and Aswad, D. W., Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides, J. Biol. Chem., 262, 5622, 1987.
24. Stephenson, R. C. and Clarke, S., Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins, J. Biol. Chem., 264, 6164, 1989.
25. Scotchler, J. W. and Robinson, A. B., Deamidation of glutaminyl residues: dependence on pH, temperature, and ionic strength, Anal. Biochem., 59, 319, 1974.
26. Jenks, H. T., Catalysis in Chemistry and Enzymology, McGraw-Hill, New York, 1969, 523.
27. Thannhauser, T. W. and Scheraga, H. A., Reversible blocking of the half cysteine residues of proteins and the irreversible specific deamidation of asparagine 67 of s-sulforibonuclease under mild conditions, Biochemistry, 24, 2581, 1985.
28. Meinwald, Y. C., Stimson, E. R., and Scheraga, H. A., Deamidation of the asparaginyl-glycyl sequence, Int. J. Peptide Protein Res., 28, 79, 1986.
29. Lura, R. and Schirch, V., Role of peptide conformation in the rate and mechanism of deamidation of asparaginyl residues, Biochemistry, 27, 7671, 1988.
30. Swallow, D. L. and Abraham, E. P., Formation of e-(amino succinyl)-lysine from e-aspartyl-lysine from bacitracin-A and from the cell walls of lactobacilli, Biochem. J., 70, 364, 1958.
31. Bernard, S. A., Carter, J. H., Katchalski, E., Sela, M., and Shalitin, Y., Cooperative effects of functional groups in peptides. I. Aspartyl-serine derivatives, J. Am. Chem. Soc., 84, 2421, 1962.
32. Ondetti, M. A., Deer, A., Sheehan, J. T., Pluscec, J., and Koey, O., Side reactions in synthesis of peptide containing aspartyl glycyl sequence, Biochemistry, 7, 4069, 1968.
33. Bodanszky, M. and Kwei, J. Z., Side reactions in peptide synthesis. VII. Sequence dependence in formation of aminosuccinyl derivatives from b-benzylaspartyl peptides, Int. J. Peptide Protein Res., 12, 69, 1978.
34. Sondheimer, E. and Holley, R. W., Imides from asparagine and glutamine, J. Am. Chem. Soc., 76, 2467, 1954.
35. Bhatt, N. P., Patel, K., and Borchardt, R. T., Chemical pathways of peptide degradation. I. Deamidation of adrenocorticotropic hormone, Pharm. Res., 7, 593, 1990.
36. Patel, K. and Borchardt, R. T., Chemical pathways of peptide degradation. III. Effect of primary sequence on the pathways of deamidation of asparaginyl residues in hexapeptides, Pharm. Res., 7, 787, 1990.
37. Naughton, M. A., Sanger, F., Hartley, B. S., and Shaw, D. C., Amino acid sequence around reactive serine residues of some proteolytic enzymes, Biochem. J., 77, 149, 1960.
38. Aswad, D. W., Johnson, B. A., Langmack, E. L., and Shirokawa, J., Modification of isoaspartyl peptides and proteins by protein carboxyl methyltransferase from bovine brain, in Advances in Post-Translational Modification of Proteins and Aging, Zappia, V., Galletti, P., and Porta, R., Eds., Plenum Press, New York, 1988, 247.
39. Capasso, S., Mazzarella, L., Sica, F., and Zagari, A., Deamidation via cyclic imide in asparaginyl peptides, Peptide Res., 2, 195, 1989.
40. Robinson, A. B., Scotchler, J. W., and McKerrow, J. H., Rates of nonenzymatic deamidation of glutaminyl and asparaginyl residues in pentapeptides, J. Am. Chem. Soc., 95, 8156, 1973.
41. Melville, J., Labile glutamine peptides and their bearing on the origin of the ammonia set tree during the enzymatic digestion of proteins, Biochem. J., 29, 179, 1935.
42. Leach, S. J. and Lindley, H., The kinetics of hydrolysis of the amide group in proteins and peptides. II. Acid hydrolysis of glycyl-L-asparagine and L-leucyl-L-asparagine, Trans. Faraday Soc., 49, 921, 1953.
43. Slobin, L., The Action of Carboxypeptidase-A on Bovine Insulin and Related Model Peptides, Dissertation, University of California, Berkeley, 1964.
44. Carpenter, F. H., Relationship of structure to biological activity of insulin as revealed by degradative studies, Am. J. Med., 40, 750, 1966.
45. Markussen, J., Diers, I., Hougaard, P., Langkjaer, L., Norris, K., Snel, L., Sorensen, A. R., Sorensen, E., and Voigt, H. O., Soluble prolonged-acting insulin derivatives. III. Degree of protraction, crystallizability and chemical stability of insulins substituted in positions A21, B13, B23, B27, and B30, Protein Eng., 2, 157, 1988.
46. Wright, H. T. and Robinson, A. B., Cryptic amidase active sites catalyze deamidation in proteins, in From Cyclotrons to Cytochromes, Kaplan, N. O. and Robinson, A. B., Eds., Academic Press, New York, 1982, 727.
47. Kossiakoff, A. A., Tertiary structure is a principal determinant to protein deamidation, Science, 240, 191, 1988.
48. Clarke, S., Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins, Int. J. Peptide Protein Res., 30, 808, 1987.
49. Wearne, S. J. and Creighton, T. E., Effect of protein conformation on rate of deamidation: ribonuclease A, Protein Struct. Funct. Gen., 5, 8, 1989.
50. Ma, C. Y. and Khanzada, G., Functional properties of oat protein isolates, J. Food Sci., 52, 1583, 1987.
51. Kato, A., Tsutsui, N., Matsudomi, K., Kobauashi, K., and Nakai, S., Effects of partial denaturation on surface properties of ovalbumin and lysozyme, Agric. Biol. Chem., 45, 2755, 1981.
52. Hamada, J. S., Shih, F. F., Frank, A. W., and Marshall, W. E., Deamidation of soy peptides and proteins by bacillus circulans peptidoglutaminase, J. Food Sci., 53, 671, 1988.
53. Hamada, J. S. and Marshall, W. E., Enhancement of peptidoglutaminase deamidation of soy protein by heat treatment and/or proteolysis, J. Food Sci., 53, 1132, 1988.
54. Hamada, J. S., Effects of heat and proteolysis on deamidation of food proteins using peptidoglutaminase, J. Agric. Food Chem., 40, 719, 1992.
55. Motoki, M., Seguro, K., Nio, N., and Takinami, K., Glutamine-specific deamidation of as 1-casein by transglutaminase, Agric. Biol. Chem., 50, 3025, 1986.
56. Matsudomi, N., Tanaka, A., Kato, A., and Kohayashi, K., Functional properties of deamidated gluten obtained by treating with chymotrypsin at alkali pH, Agric. Biol. Chem., 1986, 50, 1989.
57. Holme, J. and Briggs, D. R., Studies on the physical nature of gliadin, Cereal Chem., 36, 321, 1959.
58. MacDonald, C. E. and Pence, J. W., Wheat gliadin in foams for food products, Food Technol., 15, 141, 1961.
59. Gagen, W. L. and Holme, J., in Industrial Use of Cereals, Pomeranz, Y., Ed., American Association of Cereal Chemists, St. Paul, MN, 1973, 8.
60. Melnychyn, P. and Pollack, C. L., Protein, Canadian Patent no. 897, 1972, 152.
61. Horiuchi, T., Fukishima, D., Sugimoto, H., and Hattori, T., Food Chem., 3, 35, 1978.
62. Kato, A. and Nakai, S., Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta, 624, 13, 1980.
63. Gilbert, J. B., Price, V. E., and Greenstein, J. P., Effect of anions on the nonenzymatic deamidation of glutamine. J. Biol. Chem., 180, 209, 1949.
64. Steinhardt, J. and Fugitt, C. H., Catalyzed hydrolysis of amide and peptide bonds in proteins, J. Res. Natl. Bur. Stand., 29, 315, 1942.
65. Shih, F. F. and Kalmar, A. D., SDS-catalyzed deamidation of soy proteins, J. Agric. Food Chem., 35, 672, 1987.
66. Shih, F. F., Deamidation of protein in a soy extract by ion exchange resin catalysis, J. Food Sci., 52, 1529, 1987.
67. Zhang, J., Lee, T. C., and Ho, C.-T., Thermal deamidation of proteins in a restricted water environment, J. Agric. Food Chem., 41, 1840, 1993.
68. Izzo, H. V., The Nonenzymatic Deamidation of Wheat Proteins during Extrusion: Studies on the Occurrence, Catalysis, and Implications of Amide Loss in Foods during Processing, Ph.D. dissertation, Rutgers University, 1993.
69. Batey, I. L., Chemical modification as a probe of gluten structure, Ann. Technol. Agric., 29, 363, 1980.
70. Gebhardt, E., Neumann, C., and Eckert, I., Modification and derivatization of gluten and influence on the manufacture of baked goods, Backer Konditor, 30, 37, 1982.
71. Cunningham, D. K., Geddes, W. F., and Anderson, J. A., Preparation and chemical characteristics of cohesive proteins of wheat, barley, rye, and oats, Cereal Chem., 32, 91, 1955.
72. Kahn, K. and Bushuk, W., Structure of wheat gluten in relation to functionality in breadmaking, ACS Symp. Ser., 92, 191, 1979.
73. Wall, J. S., The role of wheat proteins in determining baking quality, in Recent Advances in the Biochemistry of Cereals, Laidman, D. L. and Jones, R. G., Eds., Academic Press, New York, 1979, 275.
74. Cheftel, J. C., Nutritional effects of extrusion-cooking, Food Chem., 20, 263, 1986.
75. Camire, M. E., Camire, A., and Krumhar, H., Chemical and nutritional changes in foods during extrusion, Crit. Rev. Food Sci. Nutr., 29, 35, 1990.
76. Izzo, M. T., Lipid-Protein and Lipid-Carbohydrate Interactions during Twin Screw Extrusion of Corn Meal, Ph.D. dissertation. Rutgers University, 1989.
77. Wen, L. F., Rodis, P., and Wasserman, B. P., Starch fragmentation and protein insolubilization during twin screw extrusion of corn meal, Cereal Chem., 67, 268, 1990.
78. Izzo, H. V. and Ho, C.-T., Isolation and identification of the volatile components of an extruded autolyzed yeast extract, J. Agric. Food Chem., 39, 2245, 1991.
79. Izzo, H. V. and Ho, C.-T., Ammonia affects Maillard chemistry of an extruded autolyzed yeast extract: pyrazine aroma generation and brown color formation, J. Food Sci., 57, 657, 1992.
80. Nursten, H. E., in Developments in Food Flavours, Birch, G. G. and Lindley, M. G., Eds., Elsevier, New York, 1986, 173.
81. Hodge, J. E., Dehydrated foods: chemistry of browning reactions in model systems, J. Agric. Food Chem., 1, 928, 1953.
82. Hodge, J. E., Nonenzymatic browning reactions, in Chemistry and Physiology of Flavors, Schultz, H. W., Day, E. A., and Libbey, L. M., Eds., AVI, Westport, CT, 1967, 465.
83. Buttery, R. G., Guadagni, D. G., and Ling, L. C., Volatile compounds of baked potatoes, J. Sci. Food Agric., 24, 1125, 1973.
84. Vitzthum, O. G. and Werkoff, P., Cycloalkylpyrazines in coffee aroma, J. Agric. Food Chem., 23, 510, 1973.
85. Walradt, J. P., Lindsay, R. C., and Libbey, L. M., Popcorn flavor: identification of volatile compounds, J. Agric. Food Chem., 18, 926, 1970.
86. Walradt, J. P., Pitter, A. O., Kinlin, T. E., Muralidhara, R., and Sanderson, A., Volatile components of roasted peanuts, J. Agric. Food Chem., 19, 972, 1971.
87. Van Praag, M., Stein, H. S., and Tibbetts, M. S., Steam volatile aroma constituents of roasted cocoa beans, J. Agric. Food Chem., 16, 1005, 1968.
88. Wang, P. S., Kato, H., and Fugimaki, M., Studies on the flavor components of roasted barley. III. The major volatile basic compounds, Agric. Biol. Chem., 33, 1775, 1969.
89. Koehler, P. E., Mason, M. E., and Newell, J. A., Formation of pyrazine compounds in sugar-amino acid model systems, J. Agric. Food Chem., 17, 393, 1969.
90. Hwang, H.-I., Hartman, T. G., Rosen, R. T., and Ho, C.-T., Formation of pyrazines from the Maillard reaction of glucose and glutamine-amide-15N, J. Agric. Food Chem., 41, 2122, 1993.
91. Lorand, L., The fibrin-stabilizing factor system of blood plasma, Ann. N.Y. Acad. Sci., 202, 6, 1972.
92. Mosher, D. F., Schad, P. E., and Kleinman, J., Cross-linking of fibronectin to collagen by blood coagulation factor XIIa, Clin. Invest., 64, 781, 1979.
93. Motoki, M. and Nio, N., Crosslinking between different food proteins by transglutaminase, J. Food Sci., 48, 561, 1983.
94. Tanimoto, S. Y. and Kinsella, J. E., Enzymatic modification of proteins: Effects of transglutaminase cross-linking on some physical properties of β-lactoglobulin, J. Agric. Food Chem., 36, 281, 1988.
95. Ikura, K., Kometani, T., Yoshikawa, M., Sasaki, R., and Chiba, H., Cross-linking of soybean 7S and 11S proteins by transglutaminase, Agric. Biol. Chem., 44, 2979, 1980.
96. Ikura, K., Yoshikawa, M., Sasaki, R., and Chiba, H., Incorporation of amino acids into food proteins by transglutaminase, Agric. Biol. Chem., 45, 2587, 1981.
97. Otterburn, M. S., Healy, M., and Sinclair, W., Protein crosslinking, in Adv. Exp. Med. Biol. 86, Friedman, M., Ed., Plenum, New York, 1977, 239.
98. Zhang, J., Lee, T. C., and Ho, C.-T., Kinetics and mechanism of nonenzymatic deamidation of soy protein, J. Food Process. Presv., 17, 259, 1993.
99. Zhang, J., Lee, T. C., and Ho, C.-T., Comparative study on kinetics of nonenzymatic deamidation of soy protein and egg white lysozyme, J. Agric. Food Chem., 41, 2286, 1993.
100. Patel, K. and Borchardt, R. T., Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide, Pharm. Res., 7, 703, 1990.
101. Leach, S. J. and Lindley, H., The kinetics of hydrolysis of the amide group in proteins and peptides. I. The acid hydrolysis of L-asparagine and L-asparaginylglycine, Trans Faraday Soc., 49, 915, 1953.
102. Snyder, H. E. and Kwon, T. W., Morphology and composition, in Soybean Utilization, Van Nostrand Reinhold, New York, 1987, 46.