Glycation a promising method for food protein modification: Physicochemical properties and structure, a review

Food Research International

Volumn 49, Issue 1, 2012, Pages 170-183

  Liu, Jianhua ^a   Ru, Qiaomei ^a   Ding, Yuting ^a  

^a ZHEJIANG UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Food protein; Glycation; Maillard reaction; Physicochemical properties; Structure; Structure function relationship

Indexed keywords

FOOD PROTEINS; GLYCATION; MAILLARD REACTION; PHYSICOCHEMICAL PROPERTY; STRUCTURE-FUNCTION RELATIONSHIP;

CARBOHYDRATES; CHEMICAL CONTAMINATION; CHEMICAL REACTIONS; GLYCOSYLATION; PROTEINS; RESEARCH; STRUCTURE (COMPOSITION);

STRUCTURAL PROPERTIES;

EID: 84866028087     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2012.07.034     Document Type: Review

References (140)

1. Achouri A., Boye J.I., Belanger D., Chiron T., Yaylayan V.A., Yeboah F.K. Functional and molecular properties of calcium precipitated soy glycinin and the effect of glycation with κ-carrageenan. Food Research International 2010, 43:1494-1504.
2. Achouri A., Boye J.I., Yaylayan V.A., Yeboah F.K. Functional properties of glycated soy 11S glycinin. Journal of Food Science 2005, 70:269-274.
3. ε-(carboxymethyl) lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochemical Journal 1997, 324:565-570.
4. Alizadeh-Pasdar N., Li-Chan E.C.Y. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry 2000, 48:328-334.
5. Ames J.M. The Maillard reaction. Biochemistry of food proteins 1992, 99-153. Elsevier Science Publishers, London. B.J.F. Hudson (Ed.).
6. Aoki S., Hasegawa G., Shigeta H., Obayashi H., Fujii M., Kimura F., et al. Crossline levels in serum and erythrocyte membrane proteins from patients with diabetic nephropathy. Diabetes Research and Clinical Practice 2000, 48:119-125.
7. Aoki T., Hiidome Y., Kitahata K., Sugimoto Y., Ibrahim H.R., Kato Y. Improvement of heat stability and emulsifying activity of ovalbumin by conjugation with glucuronic acid through the Maillard reaction. Food Research International 1999, 32:129-133.
8. Arntfield S.D., Murray E.D. The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Journal-Canadian Institute of Food Science and Technology 1981, 14:289-294.
9. Ashie I.N.A., Lanier T.C. High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase. Journal of Food Science 1999, 64:704-708.
10. Baniel A., Caer D., Colas B., Gueguen J. Functional properties of glycosylated derivatives of the 11S storage protein from pea (Pisum sativum L.). Journal of Agricultural and Food Chemistry 1992, 40:200-205.
11. Bravo F.I., Villamiel M., Molina E. Emulsifying properties of α-lactalbumin after high pressure treatment and subsequent lactosylation. High Pressure Research 2007, 27:115-119.
12. Bunn H.F., Shapiro R., McManus M., Garrick L., McDonald M.J., Gallop P.M., et al. Structural heterogeneity of human haemoglobin A due to nonenzymatic glycosylation. Journal of Biological Chemistry 1979, 254:3892-3898.
13. Caer D., Baniel A., Subirade M., Gueguen J., Colas B. Preparation and physicochemical properties of glycosylated derivatives of pea legumin. Journal of Agricultural and Food Chemistry 1990, 38:1700-1706.
14. Campbell L., Raikos V., Euston S.E. Modification of functional properties of egg-white proteins. Nahrung 2003, 47:369-376.
15. Cardamone M., Puri N. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochemical Journal 1992, 282:589-593.
16. Cardoso J.C., Albuquerque R.L.C., Padilha F.F., Bittencourt F.O., De Freitas O., Nunes P.S., et al. Effect of the Maillard reaction on properties of casein and casein films. Journal of Thermal Analysis and Calorimetry 2011, 104:249-254.
17. Carulli S., Calvano C.D., Palmisano F. MALDI-TOF MS characterization of glycation products of whey proteins in a glucose/galactose model system and lactose-free milk. Journal of Agricultural and Food Chemistry 2011, 59:1793-1803.
18. Chevalier F., Chobert J.M., Dalgalarrondo M., Choiset Y., Haertlé T. Maillard glycation of β-lactoglobulin induces conformation changes. Nahrung 2002, 46:58-63.
19. Chevalier F., Chobert J.M., Genot C., Haertlé T. Scavenging of free radicals, antimicrobial, and cytotoxic activities of the Maillard reaction products of β-lactoglobulin glycated with several sugars. Journal of Agricultural and Food Chemistry 2001, 49:5031-5038.
20. Chevalier F., Chobert J.M., Popineau Y., Nicolas M.G., Haertlé T. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. International Dairy Journal 2001, 11:145-152.
21. Chobert J.M., Gaudin J.C., Dalgalarrondo M., Haertlé T. Impact of Maillard type glycation on properties of beta-lactoglobulin. Biotechnology Advances 2006, 24:629-632.
22. Christopher P., Stowell P., Lee Y.C. Neoglycoproteins. The preparation and application of synthetic glycoproteins. Advances in Carbohydrate Chemistry and Biochemistry 1980, 37:225-281.
23. Colas B., Caer D., Fournier E. Transglutaminase-catalyzed glycosylation of vegetable proteins. Effect on solubility of pea legumin and wheat gliadines. Journal of Agricultural and Food Chemistry 1993, 41:1811-1815.
24. Corzo-Martínez F., Moreno F.J., Olano A., Villamiel M. Structural characterization of bovine β-lactoglobulin-galactose/tagatose Maillard complexes by electrophoretic, chromatographic, and spectroscopic methods. Journal of Agricultural and Food Chemistry 2008, 56:4244-4252.
25. Corzo-Martínez M., Moreno F.J., Olano A., Villamiel M. Role of pyridoxamine in the formation of the Amadori/Heyns compounds and aggregates during the glycation of β-lactoglobulin with galactose and tagatose. Journal of Agricultural and Food Chemistry 2010, 58:500-506.
26. Corzo-Martínez M., Moreno F.J., Villamiel M., Harte F.M. Characterization and improvement of rheological properties of sodium caseinate glycated with galactose, lactose and dextran. Food Hydrocolloids 2010, 24:88-97.
27. Damodaran S. Amino acids, peptides, and proteins. Food chemistry 1996, 321-429. Marcel Dekker, New York. O.R. Fennema (Ed.).
28. Darewicz M., Dziuba J. The effect of glycosylation on emulsifying and structural properties of bovine β-casein. Nahrung 2001, 45:15-20.
29. Darewicz M., Dziuba J., Mioduszewska H. Some physico-chemical properties and structural changes of bovine β-casein upon glycation. Nahrung 1998, 42:213-214.
30. Decourcelle N., Sabourin C., Dauer G., Guérard F. Effect of the Maillard reaction with xylose on the emulsifying properties of a shrimp hydrolysate (Pandalus borealis). Food Research International 2010, 43:2155-2160.
31. Dickinson E., Izgi E. Foam stabilization by protein-polysaccharide complexes. Colloids and Surfaces A: Physicochemical and Engineering Aspects 1996, 113:191-201.
32. Diftis N., Kiosseoglou V. Competitive adsorption between a dry-heated soy protein-dextran mixture and surface-active materials in oil-in-water emulsions. Food Hydrocolloids 2004, 18:639-646.
33. Dyer D.G., Blackledge J.A., Thorpe S.R., Baynes J.W. Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. Journal of Biological Chemistry 1991, 266:11654-11660.
34. Easa A.M., Hill S.E., Mitchell J.R., Taylor A.J. Bovine serum albumin gelation as a result of the Maillard reaction. Food Hydrocolloids 1996, 10:199-202.
35. Farhat I.A., Orset S., Moreau P., Blanshard J.M.V. FTIR study of hydration phenomena in protein-sugar systems. Journal of Colloid and Interface Science 1998, 207:200-208.
36. Fenaille F., Morgan F., Parisod V., Tabet J.C., Guy P.A. Solid-state glycation of β-lactoglobulin monitored by electrospray ionisation mass pectrometry and gel electrophoresis techniques. Rapid Communications in Mass Spectrometry 2003, 17:1483-1492.
37. Francois F., Campos-Giménez E., Guy P.A., Schmitt C., Morgan F. Monitoring of β-lactoglobulin dry-state glycation using various analytical techniques. Analytical Biochemistry 2003, 320:144-148.
38. French S.J., Harper W.J., Kleinholz N.M., Jones R.B., Green-Church K.B. Maillard reaction induced lactose attachment to bovine β-lactoglobulin: Electrospray ionization and matrix-assisted laser desorption/ionization examination. Journal of Agricultural and Food Chemistry 2002, 50:820-823.
39. Friedman M. Nutritional value of proteins from different food sources. A review. Journal of Agricultural and Food Chemistry 1996, 44:6-29.
40. Friedman M. Food browning and its prevention: An overview. Journal of Agricultural and Food Chemistry 1996, 44:631-653.
41. Fujiwara K., Oosawa T., Saeki H. Improved thermal stability and emulsifying properties of carp myofibrillar proteins by conjugation with dextran. Journal of Agricultural and Food Chemistry 1998, 46:1257-1261.
42. Garcia R.N., Adachi M., Tecson-Mendoza E.M., Bernardo A.E.N., Utsumi S. Physicochemical properties of native and recombinant mungbean (Vigna radiate L. Wilczek) 8S globulins and the effects of the N-linked glycans. Journal of Agricultural and Food Chemistry 2006, 54:6005-6010.
43. Gasymov O.K., Glasgow B.J. ANS fluorescence: Potential to augment the identification of the external binding sites of proteins. Biochimica et Biophysica Acta 2007, 1774:403-411.
44. Georget D.M.R., Belton P.S. Effects of temperature and water content on the secondary structure of wheat gluten studied by FTIR spectroscopy. Biomacromolecules 2006, 7:469-475.
45. Gerrard J.A., Brown P.K., Fayle S.E. Maillard crosslinking of food proteins III: The effects of gluteraldehyde, formaldehyde and glyceraldehydes upon bread and croissants. Food Chemistry 2003, 80:45-50.
46. Grandhee S.K., Monnier V.M. Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. Journal of Biological Chemistry 1991, 266:11649-11653.
47. Groubet R., Chobert J.M., Haertlé T. Functional properties of milk proteins glycated in mild conditions. Sciences des Aliments 1999, 19:423-438.
48. Gu F.L., Kim J.M., Abbas S., Zhang X.M., Xia S.Q., Chen Z.X. Structure and antioxidant activity of high molecular weight Maillard reaction products from casein-glucose. Food Chemistry 2010, 120:505-511.
49. Haar R.T., Schols H.A., Gruppen H. Effect of saccharide structure and size on the degree of substitution and product dispersity of α-lactalbumin glycated via the Maillard reaction. Journal of Agricultural and Food Chemistry 2011, 59:9378-9385.
50. Haar R.T., Westphal Y., Wierenga P.A., Schols H.A., Gruppen H. Cross-linking behavior and foaming properties of bovine α-lactalbumin after glycation with various saccharides. Journal of Agricultural and Food Chemistry 2011, 59:12460-12466.
51. Hattori M., Aiba Y., Nagasawa K., Takahashi K. Functional improvement of alginic acid by conjugating with β-lactoglobulin. Journal of Food Science 1996, 61:1171-1176.
52. Hattori M., Nagasawa K., Ametani A., Kaminogawa S., Takahashi K. Functional changes in β-lactoglobulin by conjugation with carboxymethyl dextran. Journal of Agricultural and Food Chemistry 1994, 42:2120-2125.
53. Hattori M., Ogino A., Nakai H., Takahashi K. Functional improvement of β-lactoglobulin by conjugating with alginate lyase-lysate. Journal of Agricultural and Food Chemistry 1997, 45:703-708.
54. Hayakawa S., Nakai S. Relationship of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 1985, 50:486-491.
55. Herh P.K.W., Colo S.M., Roye N., Hedman K. Rheology of foods: New techniques, capabilities, and instruments. American Laboratory 2000, 32:16-20.
56. Hirayama Y., Watabe S. Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle. European Journal of Biochemistry 1997, 246:380-387.
57. Hodge J.E. Chemistry of browning reactions in model systems. Journal of Agricultural and Food Chemistry 1953, 1:928-943.
58. Jiménez-Castaño L., López-Fandiño R., Olano A., Villamiel M. Study on β-lactoglobulin glycosylation with dextran: Effect on solubility and heat stability. Food Chemistry 2005, 93:689-695.
59. Jiménez-Castaño L., Villamiel M., López-Fandiño R. Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass. Food Hydrocolloids 2007, 21:433-443.
60. Jiménez-Castaño L., Villamiel M., Martín-Álvarez P.J., Olano A., López-Fandiño R. Effect of the dry-heating conditions on the glycosylation of β-lactoglobulin with dextran through the Maillard reaction. Food Hydrocolloids 2005, 19:831-837.
61. Johnson W.C. Protein secondary structure and circular dichroism: A practical guide. Proteins: Structure Function and Genetics 1990, 7:205-214.
62. Kahn P.C. The interpretation of near-ultraviolet circular dichroism. Methods in Enzymology 1979, 61:339-378.
63. Katayama S., Shima J., Saeki H. Solubility improvement of shellfish muscle proteins by reaction with glucose and its soluble state in low-ionic strength medium. Journal of Agricultural and Food Chemistry 2002, 50:4327-4332.
64. Khan T.A., Amani S., Naeem A. Glycation promotes the formation of genotoxic aggregates in glucose oxidase. Amino Acids 2012, 43(3):1311-1322.
65. Kislinger T., Humeny A., Pischetsrieder M. Analysis of protein glycation products by matrix-assisted laser desorption ionization time-of flight mass spectrometry. Current Medicinal Chemistry 2004, 11:2185-2193.
66. Kitabatake N., Cuq J.L., Cheftel J.C. Covalent binding of glycosyl residues to β-lactoglobulin: Effects on solubility and heat stability. Journal of Agricultural and Food Chemistry 1985, 33:125-130.
67. Labuza T.P., Baisier W.M. The kinetics of nonenzymatic browning. Physical chemistry of foods 1992, 595-649. Marcel Dekker, New York. H.G. Schwartberg, R.W. Hartel (Eds.).
68. Ledl F., Schleicher E. New aspects of the Maillard reaction in foods and in the human body. Angewandte Chemie 1990, 29:565-594.
69. Lertittikul W., Benjakul S., Tanaka M. Characteristics and antioxidative activity of Maillard reaction products from a porcine plasma protein-glucose model system as influenced by pH. Food Chemistry 2007, 100:669-677.
70. Li Z., Luo Y.K., Feng L.G. Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose. European Food Research and Technology 2011, 233:387-394.
71. Machado A.P., Pinto R.S., Moysés Z.P., Nakandakare E.R., Quintão E.C.R., Passarelli M. Aminoguanidine and metformin prevent the reduced rate of HDL-mediated cell cholesterol efflux induced by formation of advanced glycation end products. The International Journal of Biochemistry & Cell Biology 2006, 38:392-403.
72. Maillard L.C. Action des acides amines sur les sucres. Formation des melanoidins par voie methodiqué. Comptes Rendus Hebdomadaires des Séances de I'Académie des Sciences 1912, 154:66-68.
73. Maitena U., Katayama S., Sato R., Saeki H. Improved solubility and stability of carp myosin by conjugation with alginate oligosaccharide. Fisheries Science 2004, 70:896-902.
74. Martins S.I.F.S., Jongen W.M.F., Van Boekel M.A.J.S. A review of Maillard reaction in food and implications to kinetic modeling. Trends in Food Science and Technology 2001, 11:364-373.
75. Medrano A., Abirached C., Panizzolo L., Moyna P., Añón M.C. The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chemistry 2009, 113:127-133.
76. Méndez J.D., Leal L.I. Inhibition of in vitro pyrraline formation by -arginine and polyamines. Biomedicine and Pharmacotherapy 2004, 58:598-604.
77. Miyata S., Monnier V.M. Immunohistochemical detection of advanced glycosylation end products in diabetic tissues using monoclonal antibody to pyrraline. Journal of Clinical Investigation 1992, 89:1102-1112.
78. Moore C., Fasman G.D. The random coil conformation of proteins. Chemtracts: Biochemistry and Molecular Biology 1993, 4:67-74.
79. Morgan F., Léonil J., Mollé D., Bouhallab S. Modification of bovine β-Lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation. Journal of Agricultural and Food Chemistry 1999, 47:83-91.
80. Morgan F., Mollé D., Henry G., Vénien A., Léonil J., Peltre G., et al. Glycation of bovine β-Lactoglobulin: Effect on the protein structure. International Journal of Food Science and Technology 1999, 34:429-435.
81. Nacka F., Chobert J.M., Burova T., Léonil J., Haertlé T. Induction of new physicochemical and functional properties by the glycosylation of whey proteins. Journal of Protein Chemistry 1998, 17:495-503.
82. Nagaraj R.H., Monnier V.M. Isolation and characterization of a blue fluorophore from human eye lens crystallins: In vitro formation from Maillard reaction with ascorbate and ribose. Biochimica et Biophysica Acta 1992, 1116:34-42.
83. Nagaraj R.H., Portero-Otin M., Monnier V.M. Pyrraline ether crosslinks as a basis for protein crosslinking by the advanced Maillard reaction in aging and diabetes. Archives of Biochemistry and Biophysics 1996, 325:152-158.
84. Nagasawa K., Takahashi K., Hattori M. Improved emulsifying properties of lactoglobulin by conjugating with carboxymethyl dextran. Food Hydrocolloids 1996, 10:63-67.
85. Nakai S. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. Journal of Agricultural and Food Chemistry 1983, 31:676-683.
86. Nakamura S., Ogawa M., Nakai S., Kato A., Kitts D. Antioxidant activity of a Maillard-type phosvitin-galactomannan conjugate with emulsifying properties and heat stability. Journal of Agricultural and Food Chemistry 1998, 46:3958-3963.
87. Niu L.Y., Jiang S.T., Pan L.J., Zhai Y.S. Characteristics and functional properties of wheat germ protein glycated with saccharides through Maillard reaction. International Journal of Food Science and Technology 2011, 46:2197-2203.
88. O'Regan J., Mulvihill D.M. Preparation, characterisation and selected functional properties of sodium caseinate-maltodextrin conjugates. Food Chemistry 2009, 115:1257-1267.
89. Obayashi H., Nakano K., Shigeta H., Yamaguchi M., Yoshimori K., Fukui M., et al. Formation of crossline as a fluorescent advanced glycation end product in vitro and in vivo. Biochemical and Biophysical Research Communications 1996, 226:37-41.
90. Oliver C.M. Insight into the glycation of milk proteins, an ESI-and MALDI-MS perspective (review). Critical Reviews in Food Science and Nutrition 2011, 51:410-431.
91. Oliver C.M., Kher A., McNaughton D., Augustin M.A. Use of FTIR and mass spectrometry for characterization of glycated caseins. The Journal of Dairy Research 2009, 76:105-110.
92. Oliver C.M., Stanley R.A., Melton L.D. Creating proteins with novel functionality through the Maillard reaction. Critical Reviews in Food Science and Nutrition 2006, 46:337-350.
93. Paraman I., Hettiarachchy N.S., Schaefer C. Glycosylation and deamidation of rice endosperm protein for improved solubility and emulsifying properties. Cereal Chemistry 2007, 84:593-599.
94. Pedrosa C., De Felice F., Trisciuzzi C., Ferreira S. Selective neoglycation increases the structural stability of vicilin, the 7S storage globulin from pea seeds. Archives of Biochemistry and Biophysics 2000, 382:203-210.
95. Pedrosa C., Trisciuzzi C., Ferreira S.T. Effects of glycosylation on functional properties of vicilin, the 7S storage globulin from pea (Pisum sativum). Journal of Agricultural and Food Chemistry 1997, 45:2025-2030.
96. Privalov P.L. Stability of proteins: Proteins which do not present a single cooperative system. Advances in Protein Chemistry 1982, 35:1-104.
97. Qi J.R., Yang X.Q., Liao J.S. Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction. International Journal of Food Science and Technology 2009, 44:2296-2302.
98. Rizzi G.P. Chemical structure of coloured Maillard reactions products. Food Reviews International 1997, 13:1-28.
99. Saeki H., Inoue K. Improved solubility of carp myofibrillar proteins in low ionic strength medium by glycosylation. Journal of Agricultural and Food Chemistry 1997, 45:3419-3422.
100. Sanmartín E., Arboleya J.C., Moreno F.J. Recent advances in the recovery and improvement of functional proteins from fish processing by-products: Use of protein glycation as an alternative method. Comprehensive Reviews in Food Science and Food Safety 2009, 8:332-344.
101. Sanz M.L., Corzo-Martínez M., Rastall R.A., Olano A., Moreno F.J. Characterization and in vitro digestibility of bovine β-lactoglobulin glycated with galactooligosaccharides. Journal of Agricultural and Food Chemistry 2007, 55:7916-7925.
102. Sato R., Katayama S., Sawabe T., Saeki H. Stability and emulsion-forming ability of water-soluble fish myofibrillar protein prepared by conjugation with alginate oligosaccharide. Journal of Agricultural and Food Chemistry 2003, 51:4376-4381.
103. Sato R., Sawabe T., Kishimura H., Hayashi K., Saeki H. Preparation of neoglycoprotein from carp myofibrillar protein and alginate oligosaccharide: Improved solubility in low ionic strength medium. Journal of Agricultural and Food Chemistry 2000, 48:17-21.
104. Sato R., Sawabe T., Saeki H. Characterization of fish myofibrillar protein by conjugation with alginate oligosaccharide prepared using genetic recombinant alginate lyase. Journal of Food Science 2005, 70:58-62.
105. Sava N., Plancken V. The kinetics of heat-induced structural changes of β-lactoglobulin. Journal of Dairy Science 2005, 88:1646-1653.
106. Shepherd R., Robertson A., Ofman D. Dairy glycoconjugate emulsifiers: Casein-maltodextrins. Food Hydrocolloids 2000, 14:281-286.
107. Song Y., Babiker E.E., Usui M., Saito A., Kato A. Emulsifying properties and bactericidal action of chitosan-lysozyme conjugates. Food Research International 2002, 35:459-466.
108. Strickland E.H. Aromatic contribution to circular dichroism spectra of proteins. Critical Reviews in Biochemistry and Molecular Biology 1974, 2:113-175.
109. Sun Y.X., Hayakawa S., Izumori K. Antioxidative activity and gelling rheological properties of dried egg white glycated with a rare ketohexose through the Maillard reaction. Journal of Food Science 2004, 69:427-434.
110. Sun Y.X., Hayakawa S., Izumori K. Modification of ovalbumin with a rare ketohexose through the Maillard reaction: Effect on protein structure and gel properties. Journal of Agricultural and Food Chemistry 2004, 52:1293-1299.
111. Sun Y.X., Hayakawa S., Ogawa M., Izumori K. Evaluation of the site specific protein glycation and antioxidant capacity of rare sugar-protein/peptide conjugates. Journal of Agricultural and Food Chemistry 2005, 53:10205-10212.
112. Sun Y.X., Hayakawa S., Puangmanee S., Izumori K. Chemical properties and antioxidative activity of glycated α-lactalbumin with a rare sugar, d-allose, by Maillard reaction. Food Chemistry 2006, 95:509-517.
113. Surewicz W.K., Mantsch H.H. Spectroscopic methods for determining protein structure 1996, VCH, New York.
114. Takahashi K., Lou X.F., Ishii Y., Hattori M. Lysozymeglucose stearic acid monoester conjugate formed through the Maillard reaction as an antibacterial emulsifier. Journal of Agricultural and Food Chemistry 2000, 48:2044-2049.
115. Tanaka M., Kunisaki N., Ishizaki S. Improvement of emulsifying and antibacterial properties of salmine by the Maillard reaction with dextran. Fisheries Science 1999, 65:623-628.
116. Tang C.H., Sun X., Foegeding E.A. Modulation of physicochemical and conformational properties of kidney bean vicilin (phaseolin) by glycation with glucose: Implications for structure-function relationships of legume vicilins. Journal of Agricultural and Food Chemistry 2011, 59:10114-10123.
117. Tessier F., Obrenovich M., Monnier V.M. Structure and mechanism of formation of human lens fluorophore LM-1. Relationship to vesperlysine A and the advanced Maillard reaction in aging, diabetes, and cataractogenesis. Journal of Biological Chemistry 1999, 274:20796-20804.
118. Thomsen M.K., Olsen K., Otte J., Sjøstrøm K., Werner B.B., Skibsted L.H. Effect of water activity, temperature and pH on solid state lactosylation of β-lactoglobulin. International Dairy Journal 2012, 23:1-8.
119. Tian S.J., Chen J., Small D.M. Enhancement of solubility and emulsifying properties of soy protein isolates by glucose conjugation. Journal of Food Processing and Preservation 2011, 35:80-95.
120. Turner J.A., Sivasundaram L.R., Ottenhof M.A., Farhat I.A., Linforth R.S.T., Taylor A.J. Monitoring chemical and physical changes during thermal flavor generation. Journal of Agricultural and Food Chemistry 2002, 50:5406-5411.
121. Van Boekel M.A.J.S. Kinetic aspects of the Maillard reaction: A critical review. Nahrung 2001, 45:150-159.
122. Van de Lagemaat J., Silván J.M., Moreno F.J., Olano A., Del Castillo M.D. In vitro glycation and antigenicity of soy proteins. Food Research International 2007, 40:153-160.
123. Wang Q., Ismail B. Effect of Maillard-induced glycosylation on the nutritional quality, solubility, thermal stability and molecular configuration of whey protein. International Dairy Journal 2012, 25:112-122.
124. Watabe S., Hirayama Y., Imai J., Kikuchi K., Yamashita M. Sequences of cDNA clones encoding R-actin of carp and goldfish skeletal muscles. Fisheries Science 1995, 61:998-1003.
125. Wong B.T., Day L., Augustin M.A. Deamidated wheat proteinedextran Maillard conjugates: Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocolloids 2011, 25:1424-1432.
126. Wong B.T., Day L., McNaughton D., Augustin A. The effect of Maillard conjugation of deamidated wheat proteins with low molecular weight carbohydrates on the secondary structure of the protein. Food Biophysics 2009, 4:1-12.
127. Woody R.W. Circular dichroism. Methods in Enzymology 1995, 246:34-71.
128. Wooster T.J., Augustin M.A. β-Lactoglobulin-dextran Maillard conjugates: Their effect on interfacial thickness and emulsion stability. Journal of Colloid and Interface Science 2006, 303:564-572.
129. Wooster T.J., Augustin M.A. The emulsion flocculation stability of protein-carbohydrate diblock copolymers. Journal of Colloid and Interface Science 2007, 313:665-675.
130. Wooster T.J., Augustin M.A. Rheology of whey protein-dextran conjugate films at the air/water interface. Food Hydrocolloids 2007, 21:1072-1080.
131. Xu D.X., Wang X.Y., Jiang J.P., Yuan F., Gao Y.X. Impact of whey protein-Beet pectin conjugation on the physicochemical stability of β-carotene emulsions. Food Hydrocolloids 2012, 28:258-266.
132. Xu C.H., Yu S.J., Yang X.Q., Qi J.R., Lin H., Zhao Z.G. Emulsifying properties and structural characteristics of β-conglycinin and dextran conjugates synthesised in a pressurized liquid system. International Journal of Food Science and Technology 2010, 45:995-1001.
133. Yadav M.P., Parris N., Johnston D.B., Onwulata C.I., Hicks K.B. Corn fiber gum and milk protein conjugates with improved emulsion stability. Carbohydrate Polymers 2010, 81:476-483.
134. Yadav M.P., Strahan G.D., Mukhopadhyay S., Hotchkiss A.T., Hicks K.B. Formation of corn fiber gum-milk protein conjugates and their molecular characterization. Food Hydrocolloids 2012, 26:326-333.
135. Yajima K., Onodera S., Takeda Y., Kato I., Shiomi N. Improved radical scavenging activity of β-lactoglobulin-xylobiose modified by the Maillard reaction. Journal of Applied Glycoscience 2007, 54:165-168.
136. Yang, V. C., & Langer, R. S. (1985). Rapid method for determination the isoelectric point for 582 amphoteric molecules. United States Patent No. 4666855.
137. Zayas J.F. Functionality of proteins in food 1997, 1-2. Springer-Verlag, Berlin Heidelberg, New York.
138. Zhang J.B., Wu N.N., Yang X.Q., He X.T., Wang L.J. Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis. Food Hydrocolloids 2012, 28:301-312.
139. Zhang Y., Zhang Y. Formation and reduction of acrylamide in Maillard reaction: A review based on the current state of knowledge. Critical Reviews in Food Science and Nutrition 2007, 47:521-542.
140. Zhu D., Damodaran S., Lucey J.A. Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution. Journal of Agricultural and Food Chemistry 2010, 58:2988-2994.