Advertisement

Advanced Glycation End Products (AGEs)

  • Halise Gül Akıllıoğlu
  • Vural GökmenEmail author
Chapter

Abstract

Glycation refers to the addition of a sugar moiety to a protein molecule and occurs during the Maillard reaction. Maillard reaction is initiated by the condensation of amino groups of proteins, peptides, and amino acids with carbonyl groups of reducing sugars. After subsequent elimination, degradation, and oxidation reactions in the later stages, so-called advanced glycation end products (AGEs) are formed. AGEs have been linked to many chronic and degenerative disorders and aging. The results of several animal and human studies confirm that dietary AGE levels have effects on AGE accumulation in body and further complications in degenerative diseases. In this chapter, following brief information about protein glycation, the consequences of glycation, and the contribution of dietary AGEs will be discussed. Formation routes of main glycation products in foods will be explained and their analysis methods will be summarized. Major mitigation strategies developed so far will be evaluated.

References

  1. 1.
    Henle T et al (2008) Maillard reaction of proteins and advanced glycation end products (AGEs) in food. Wiley, New Jersey, pp 215–242Google Scholar
  2. 2.
    Rahbar S et al (1969) Studies of an unusual hemoglobin in patients with diabetes mellitus. Biochem Biophys Res Commun 36(5):838–843PubMedCrossRefPubMedCentralGoogle Scholar
  3. 3.
    Monnier VM, Cerami A (1981) Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science 211(4481):491–493PubMedCrossRefPubMedCentralGoogle Scholar
  4. 4.
    Henle T (2005) Protein-bound advanced glycation end products (AGEs) as bioactive amino acid derivatives in foods. Amino Acids 29(4):313–322PubMedPubMedCentralCrossRefGoogle Scholar
  5. 5.
    Poulsen MW et al (2013) Advanced glycation end products in food and their effects on health. Food Chem Toxicol 60:10–37PubMedCrossRefGoogle Scholar
  6. 6.
    Zeng J, Davies MJ (2005) Evidence for the formation of adducts and S-(carboxymethyl)cysteine on reaction of alpha-dicarbonyl compounds with thiol groups on amino acids, peptides, and proteins. Chem Res Toxicol 18(8):1232–1241PubMedCrossRefPubMedCentralGoogle Scholar
  7. 7.
    He J et al (2013) Simultaneous determination of N ε-(carboxymethyl) lysine and N ε-(carboxyethyl) lysine in cereal foods by LC–MS/MS. Eur Food Res Technol 238(3):367–374CrossRefGoogle Scholar
  8. 8.
    van Boekel MA (2001) Kinetic aspects of the Maillard reaction: a critical review. Nahrung/Food 45:150–159PubMedCrossRefGoogle Scholar
  9. 9.
    Chevalier F et al (2001) Maillard glycation of beta-lactoglobulin with several sugars: comparative study of the properties of the obtained polymers and of the substituted sites. Dairy Sci Technol 81(C7):651–666CrossRefGoogle Scholar
  10. 10.
    Leonil J, Molle D, Fauquant J, Maubois JL, Pearce RJ, Bouhallab S (1997) Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. J Dairy Sci 80:2270–2281PubMedCrossRefGoogle Scholar
  11. 11.
    Meltretter J et al (2007) Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose. J Agric Food Chem 55(15):6096–6103PubMedCrossRefGoogle Scholar
  12. 12.
    Fogliano V, Monti SM, Visconti A, Randazzo G, Facchiano AM, Colonna G, Ritieni A (1998) Identification of a β-lactoglobulin lactosylation site. Biochim Biophys Acta 1388:295–304PubMedCrossRefGoogle Scholar
  13. 13.
    Siciliano R et al (2000) Modern mass spectrometric methodologies in monitoring milk quality. Anal Chem 72(2):408–415PubMedCrossRefGoogle Scholar
  14. 14.
    Morgan F et al (1998) Lactolation of beta-lactoglobulin monitored by electrospray ionisation mass spectrometry. Int Dairy J 8(2):95–98CrossRefGoogle Scholar
  15. 15.
    Fenaille F et al (2004) Solid-state glycation of beta-lactoglobulin by lactose and galactose: localization of the modified amino acids using mass spectrometric techniques. J Mass Spectrom 39(1):16–28PubMedCrossRefGoogle Scholar
  16. 16.
    Oliver CM (2011) Insight into the glycation of milk proteins: an ESI- and MALDI-MS perspective (review). Crit Rev Food Sci Nutr 51(5):410–431PubMedCrossRefGoogle Scholar
  17. 17.
    Labuza TP, Baisier WM (1992) The kinetics of nonenzymatic browning. In: Schwartzberg HG, Hartel RW (eds) Physical chemistry of foods. Dekker, New York, pp 595–649Google Scholar
  18. 18.
    Thomsen MK et al (2012) Effect of water activity, temperature and pH on solid state lactosylation of β-lactoglobulin. Int Dairy J 23(1):1–8CrossRefGoogle Scholar
  19. 19.
    Martinez-Alvarenga MS et al (2014) Effect of Maillard reaction conditions on the degree of glycation and functional properties of whey protein isolate – Maltodextrin conjugates. Food Hydrocoll 38(16609336):110–118CrossRefGoogle Scholar
  20. 20.
    Pan GG et al (2006) α-dicarbonyl compounds formed by nonenzymatic browning during the dry heating of caseinate and lactose. J Agric Food Chem 54(18):6852–6857CrossRefGoogle Scholar
  21. 21.
    Velisek J (2014) Saccharides. In: Velısek J (ed) The chemistry of food. Wiley, West SussexGoogle Scholar
  22. 22.
    Broersen K et al (2004) Glycoforms of ?-lactoglobulin with improved thermostability and preserved structural packing. Biotechnol Bioeng 86(1):78–87PubMedCrossRefPubMedCentralGoogle Scholar
  23. 23.
    Sun Y et al (2005) Evaluation of the site specific protein glycation and antioxidant capacity of rare sugar-protein/peptide conjugates. J Agric Food Chem 53(26):10205–10212PubMedCrossRefPubMedCentralGoogle Scholar
  24. 24.
    Fenaille F et al (2003) Solid-state glycation of beta-lactoglobulin monitored by electrospray ionisation mass spectrometry and gel electrophoresis techniques. Rapid Commun Mass Spectrom 17(13):1483–1492PubMedCrossRefPubMedCentralGoogle Scholar
  25. 25.
    Lima M et al (2009) Ultra performance liquid chromatography-mass spectrometric determination of the site specificity of modification of beta-casein by glucose and methylglyoxal. Amino Acids 36(3):475–481PubMedCrossRefPubMedCentralGoogle Scholar
  26. 26.
    Huang X et al (2013) Increase of ovalbumin glycation by the Maillard reaction after disruption of the disulfide bridge evaluated by liquid chromatography and high resolution mass spectrometry. J Agric Food Chem 61(9):2253–2262PubMedCrossRefPubMedCentralGoogle Scholar
  27. 27.
    Brown EM et al (1988) Accessibility and mobility of lysine residues in.beta.-lactoglobulin. Biochemistry 27(15):5601–5610PubMedCrossRefPubMedCentralGoogle Scholar
  28. 28.
    Sawyer L, Kontopidis G, Wu S-Y (1999) β-Lactoglobulin – a three-dimensional perspective. Int J Food Sci Technol 34:409–418CrossRefGoogle Scholar
  29. 29.
    JW B et al (1989) In: Baynes JW, Monnier VM, Liss AR (eds) The Amadori product on protein: structure and reactions, New York, pp 43–67Google Scholar
  30. 30.
    Mennella C et al (2006) Glycation of lysine-containing dipeptides. J Pept Sci 12(4):291–296PubMedCrossRefGoogle Scholar
  31. 31.
    Shilton BH, Walton DJ (1991) Sites of glycation of human and horse liver alcohol dehydrogenase in vivo. J Biol Chem 266(9):5587PubMedGoogle Scholar
  32. 32.
    Shilton BH, Campbell RL, Walton DJ (1993) Site specificity of glycation of horse liver alcohol dehydrogenase in vitro. Eur J Biochem 215(3):567–572PubMedCrossRefGoogle Scholar
  33. 33.
    Fogliano V et al (1998) Identification of a beta-lactoglobulin lactosylation site. Biochim Biophys Acta 1388:295–304PubMedCrossRefGoogle Scholar
  34. 34.
    Yeboah FK et al (2000) Monitoring glycation of lysozyme by electrospray ionization mass spectrometry. J Agric Food Chem 48(7):2766PubMedCrossRefGoogle Scholar
  35. 35.
    Baynes JW (2001) The role of AGEs in aging: causation or correlation. Exp Gerontol 36(9):1527–1537PubMedCrossRefGoogle Scholar
  36. 36.
    Henle T (2007) Dietary advanced glycation end products--a risk to human health? A call for an interdisciplinary debate. Mol Nutr Food Res 51(9):1075–1078PubMedCrossRefGoogle Scholar
  37. 37.
    Wang Z et al (2012) Advanced glycation end-product Nepsilon-carboxymethyl-Lysine accelerates progression of atherosclerotic calcification in diabetes. Atherosclerosis 221(2):387–396PubMedCrossRefGoogle Scholar
  38. 38.
    Sakata N et al (1999) Increased advanced glycation end products in atherosclerotic lesions of patients with end-stage renal disease. Atherosclerosis 142(1):67PubMedCrossRefGoogle Scholar
  39. 39.
    Münch G et al (1998) Alzheimer’s disease--synergistic effects of glucose deficit, oxidative stress and advanced glycation end products. J Neural Transm 105(4–5):439–461PubMedCrossRefGoogle Scholar
  40. 40.
    Li J et al (2012) Advanced glycation end products and neurodegenerative diseases: mechanisms and perspective. J Neurol Sci 317(1–2):1–5PubMedCrossRefPubMedCentralGoogle Scholar
  41. 41.
    Thornalley PJ et al (2003) Quantitative screening of advanced glycation end products in cellular and extracellular proteins by tandem mass spectrometry. Biochem J 375(3):581–592PubMedPubMedCentralCrossRefGoogle Scholar
  42. 42.
    Ahmed N et al (2005) Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes. Diabetologia 48(8):1590–1603PubMedCrossRefPubMedCentralGoogle Scholar
  43. 43.
    HF B et al (1978) The glycosylation of hemoglobin: relevance to diabetes mellitus. Science 200(4337):21–27CrossRefGoogle Scholar
  44. 44.
    Wells-Knecht KJ et al (1994) 3-Deoxyfructose concentrations are increased in human plasma and urine in diabetes. Diabetes 43(9):1152–1156PubMedCrossRefPubMedCentralGoogle Scholar
  45. 45.
    Schwenger V et al (2015) Advanced glycation end products (AGEs) as uremic toxins. Mol Nutr Food Res 45(3):172–176Google Scholar
  46. 46.
    Raj DS et al (2000) Advanced glycation end products: a Nephrologist’s perspective. Am J Kidney Dis 35(3):365–380PubMedCrossRefPubMedCentralGoogle Scholar
  47. 47.
    Sasaki N et al (1998) Advanced glycation end products in Alzheimer’s disease and other neurodegenerative diseases. Am J Pathol 153(4):1149–1155PubMedPubMedCentralCrossRefGoogle Scholar
  48. 48.
    Nagaraj RH et al (1991) High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Proc Natl Acad Sci U S A 88(22):10257–10261PubMedPubMedCentralCrossRefGoogle Scholar
  49. 49.
    Uribarri J et al (2005) Diet-derived advanced glycation end products are major contributors to the body’s AGE pool and induce inflammation in healthy subjects. Ann N Y Acad Sci 1043:461–466PubMedCrossRefGoogle Scholar
  50. 50.
    Roncero-Ramos I et al (2014) An advanced glycation end product (AGE)-rich diet promotes Nepsilon-carboxymethyl-lysine accumulation in the cardiac tissue and tendons of rats. J Agric Food Chem 62(25):6001–6006PubMedCrossRefPubMedCentralGoogle Scholar
  51. 51.
    Lin R-Y et al (2003) Dietary glycotoxins promote diabetic atherosclerosis in apolipoprotein E-deficient mice. Atherosclerosis 168(2):213–220PubMedCrossRefPubMedCentralGoogle Scholar
  52. 52.
    Feng JX et al (2007) Restricted intake of dietary advanced glycation end products retards renal progression in the remnant kidney model. Kidney Int 71(9):901–911PubMedCrossRefPubMedCentralGoogle Scholar
  53. 53.
    Sebekova K et al (2003) Effects of a diet rich in advanced glycation end products in the rat remnant kidney model. Am J Kidney Dis 41(3 Suppl 1):S48–S51PubMedCrossRefPubMedCentralGoogle Scholar
  54. 54.
    Somoza V et al (2006) Dose-dependent utilisation of casein-linked lysinoalanine, N(epsilon)-fructoselysine and N(epsilon)-carboxymethyllysine in rats. Mol Nutr Food Res 50(9):833–841PubMedCrossRefPubMedCentralGoogle Scholar
  55. 55.
    Harcourt BE et al (2011) Targeted reduction of advanced glycation improves renal function in obesity. Kidney Int 80(2):190–198PubMedCrossRefPubMedCentralGoogle Scholar
  56. 56.
    Koschinsky T et al (1997) Orally absorbed reactive glycation products (glycotoxins): an environmental risk factor in diabetic nephropathy. Proc Natl Acad Sci U S A 94(12):6474–6479PubMedPubMedCentralCrossRefGoogle Scholar
  57. 57.
    Uribarri J et al (2007) Circulating glycotoxins and dietary advanced glycation end products: two links to inflammatory response, oxidative stress, and aging. J Gerontol A Biol Sci Med Sci 62(4):427–433PubMedPubMedCentralCrossRefGoogle Scholar
  58. 58.
    Vlassara H et al (2002) Inflammatory mediators are induced by dietary glycotoxins, a major risk factor for diabetic angiopathy. Proc Natl Acad Sci U S A 99(24):15596–15601PubMedPubMedCentralCrossRefGoogle Scholar
  59. 59.
    Uribarri J (2003) Restriction of dietary glycotoxins reduces excessive advanced glycation end products in renal failure patients. J Am Soc Nephrol 14(3):728–731PubMedPubMedCentralCrossRefGoogle Scholar
  60. 60.
    Uribarri J et al (2003) Dietary glycotoxins correlate with circulating advanced glycation end product levels in renal failure patients. Am J Kidney Dis 42(3):532–538PubMedPubMedCentralCrossRefGoogle Scholar
  61. 61.
    Vlassara H et al (2009) Protection against loss of innate defenses in adulthood by low advanced glycation end products (AGE) intake: role of the antiinflammatory AGE receptor-1. J Clin Endocrinol Metab 94(11):4483–4491PubMedPubMedCentralCrossRefGoogle Scholar
  62. 62.
    Birlouez-Aragon I et al (2010) A diet based on high-heat-treated foods promotes risk factors for diabetes mellitus and cardiovascular diseases. Am J Clin Nutr 91(5):1220–1226PubMedCrossRefPubMedCentralGoogle Scholar
  63. 63.
    Sanz ML et al (2003) 2-Furoylmethyl amino acids and hydroxymethylfurfural as indicators of honey quality. J Agric Food Chem 51(15):4278–4283PubMedCrossRefPubMedCentralGoogle Scholar
  64. 64.
    Erbersdobler HF et al (1987) Determination of furosine in heated milk as a measure of heat intensity during processing. J Dairy Res 54(1):147–151CrossRefGoogle Scholar
  65. 65.
    Rufián-Henares JA et al (2007) Assessing nutritional quality of milk-based sport supplements as determined by furosine. Food Chem 101(2):573–578CrossRefGoogle Scholar
  66. 66.
    Delgado-Andrade C et al (2007) Lysine availability is diminished in commercial fibre-enriched breakfast cereals. Food Chem 100(2):725–731CrossRefGoogle Scholar
  67. 67.
    Castillo MDD et al (1999) Early stages of Maillard reaction in dehydrated orange juice. J Agric Food Chem 47(10):4388PubMedCrossRefPubMedCentralGoogle Scholar
  68. 68.
    Erbersdobler HF, Somoza V (2007) Forty years of furosine – forty years of using Maillard reaction products as indicators of the nutritional quality of foods. Mol Nutr Food Res 51(4):423–430PubMedCrossRefPubMedCentralGoogle Scholar
  69. 69.
    Han L et al (2013) Hydroxyl radical induced by lipid in Maillard reaction model system promotes diet-derived N(epsilon)-carboxymethyllysine formation. Food Chem Toxicol 60:536–541PubMedCrossRefPubMedCentralGoogle Scholar
  70. 70.
    Wolff SP, Dean RT (1987) Glucose autoxidation and protein modification. The potential role of ‘autoxidative glycosylation’ in diabetes. Biochem J 245(1):243–250PubMedPubMedCentralCrossRefGoogle Scholar
  71. 71.
    Glomb MA, Monnier VM (1995) Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction. J Biol Chem 270(17):10017–10026PubMedCrossRefPubMedCentralGoogle Scholar
  72. 72.
    Ahmed MU, Thorpe SR, Baynes JW (1986) Identification of N-epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 261:4889–4894PubMedPubMedCentralGoogle Scholar
  73. 73.
    Drusch S et al (1999) Determination of N ϵ -carboxymethyllysine in milk products by a modified reversed-phase HPLC method. Food Chem 65(4):547–553CrossRefGoogle Scholar
  74. 74.
    Assar SH et al (2009) Determination of Nepsilon-(carboxymethyl)lysine in food systems by ultra performance liquid chromatography-mass spectrometry. Amino Acids 36(2):317–326CrossRefGoogle Scholar
  75. 75.
    Delatour T et al (2009) Analysis of advanced glycation end products in dairy products by isotope dilution liquid chromatography-electrospray tandem mass spectrometry. The particular case of carboxymethyllysine. J Chromatogr A 1216(12):2371–2381PubMedCrossRefPubMedCentralGoogle Scholar
  76. 76.
    Fenaille F et al (2006) Modifications of milk constituents during processing: a preliminary benchmarking study. Int Dairy J 16(7):728–739CrossRefGoogle Scholar
  77. 77.
    Charissou A et al (2007) Evaluation of a gas chromatography/mass spectrometry method for the quantification of carboxymethyllysine in food samples. J Chromatogr A 1140(1–2):189–194PubMedCrossRefPubMedCentralGoogle Scholar
  78. 78.
    Hull GLJ et al (2012) Nε-(carboxymethyl)lysine content of foods commonly consumed in a Western style diet. Food Chem 131(1):170–174CrossRefGoogle Scholar
  79. 79.
    Sun X et al (2015) Formation of advanced glycation end products in ground beef under pasteurisation conditions. Food Chem 172:802–807PubMedCrossRefPubMedCentralGoogle Scholar
  80. 80.
    Wellner A et al (2011) Glycation compounds in peanuts. Eur Food Res Technol 234(3):423–429CrossRefGoogle Scholar
  81. 81.
    Zhang G et al (2011) Determination of advanced glycation end products by LC-MS/MS in raw and roasted almonds (Prunus dulcis). J Agric Food Chem 59(22):12037–12046PubMedCrossRefGoogle Scholar
  82. 82.
    Fujioka K, Shibamoto T (2004) Formation of genotoxic dicarbonyl compounds in dietary oils upon oxidation. Lipids 39(5):481PubMedPubMedCentralCrossRefGoogle Scholar
  83. 83.
    Fu MX et al (1996) The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J Biol Chem 271(17):9982–9986PubMedCrossRefGoogle Scholar
  84. 84.
    Niu L et al (2017) Free and protein-bound Nε -carboxymethyllysine and Nε -carboxyethyllysine in fish muscle: biological variation and effects of heat treatment. J Food Compost Anal 57:56–63CrossRefGoogle Scholar
  85. 85.
    Yu L et al (2016) Effect of irradiation on Nε-carboxymethyl-lysine and Nε-carboxyethyl-lysine formation in cooked meat products during storage. Radiat Phys Chem 120:73–80CrossRefGoogle Scholar
  86. 86.
    Wellner A et al (2011) Formation of Maillard reaction products during heat treatment of carrots. J Agric Food Chem 59(14):7992–7998PubMedCrossRefGoogle Scholar
  87. 87.
    Hellwig M, Henle T (2012) Quantification of the Maillard reaction product 6-(2-formyl-1-pyrrolyl)-l-norleucine (formyline) in food. Eur Food Res Technol 235(1):99–106CrossRefGoogle Scholar
  88. 88.
    Hellwig M et al (2016) Free and protein-bound Maillard reaction products in beer: method development and a survey of different beer types. J Agric Food Chem 64(38):7234–7243PubMedCrossRefGoogle Scholar
  89. 89.
    Liang Z et al (2016) Determination of free-form and peptide bound pyrraline in the commercial drinks enriched with different protein hydrolysates. Int J Mol Sci 17(7)PubMedCentralCrossRefPubMedGoogle Scholar
  90. 90.
    Somoza V et al (2005) Influence of feeding malt, bread crust, and a pronylated protein on the activity of chemopreventive enzymes and antioxidative defense parameters in vivo. J Agric Food Chem 53(21):8176PubMedCrossRefPubMedCentralGoogle Scholar
  91. 91.
    Lindenmeier M et al (2002) Structural and functional characterization of pronyl-lysine, a novel protein modification in bread crust melanoidins showing in vitro antioxidative and Phase I/II enzyme modulating activity. J Agric Food Chem 50(24):6997–7006PubMedCrossRefPubMedCentralGoogle Scholar
  92. 92.
    Lindenmeier M, Hofmann T (2004) Influence of baking conditions and precursor supplementation on the amounts of the antioxidant pronyl-L-lysine in bakery products. J Agric Food Chem 52(2):350–354PubMedCrossRefPubMedCentralGoogle Scholar
  93. 93.
    Glomb MA, Rösch D, Nagaraj RH (2001) Nδ-(5-hydroxy-4,6-dimethylpyrimidine-2-yl)-l-ornithine, a novel methylglyoxal−arginine modification in beer. J Agric Food Chem 49:366–372PubMedCrossRefPubMedCentralGoogle Scholar
  94. 94.
    Henle T et al (1997) Detection and quantification of pentosidine in foods. Zeitschrift für Lebensmitteluntersuchung und – Forschung A 204(2):95–98CrossRefGoogle Scholar
  95. 95.
    P-c C et al (2009) Analysis of glycative products in sauces and sauce-treated foods. Food Chem 113(1):262–266CrossRefGoogle Scholar
  96. 96.
    Biemel KM et al (2001) Identification and quantitative evaluation of the lysine-arginine crosslinks GODIC, MODIC, DODIC, and glucosepan in foods. Mol Nutr Food Res 45(3):210Google Scholar
  97. 97.
    Nomi Y et al (2016) Simultaneous quantitation of advanced glycation end products in soy sauce and beer by liquid chromatography-tandem mass spectrometry without ion-pair reagents and derivatization. J Agric Food Chem 64(44):8397–8405PubMedCrossRefPubMedCentralGoogle Scholar
  98. 98.
    Henle T et al (1994) Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal. Z Lebensm Unters Forsch 199(1):55–58CrossRefGoogle Scholar
  99. 99.
    Meltretter J et al (2014) Modified peptides as indicators for thermal and nonthermal reactions in processed milk. J Agric Food Chem 62(45):10903–10915PubMedCrossRefGoogle Scholar
  100. 100.
    Henle T, Zehetner G, Klostermeyer H (1995) Fast and sensitive determination of furosine. Zeitschrift Fur Lebensmittel-Untersuchung Und-Forschung 200:235–237PubMedCrossRefPubMedCentralGoogle Scholar
  101. 101.
    Troise AD et al (2015) Quantification of Nepsilon-(2-Furoylmethyl)-L-lysine (furosine), Nepsilon-(Carboxymethyl)-L-lysine (CML), Nepsilon-(Carboxyethyl)-L-lysine (CEL) and total lysine through stable isotope dilution assay and tandem mass spectrometry. Food Chem 188:357–364PubMedCrossRefPubMedCentralGoogle Scholar
  102. 102.
    Schwietzke U, Schwarzenbolz U, Henle T (2009) Influence of cheese type and maturation time on the early Maillard reaction in cheese. Czech J Food Sci 27:S140–S1S2CrossRefGoogle Scholar
  103. 103.
    Schwietzke U et al (2011) Quantification of Amadori products in cheese. Eur Food Res Technol 233(2):243–251CrossRefGoogle Scholar
  104. 104.
    Labuza TP, Saltmarch M (2010) Kinetics of browning and protein quality loss in whey powders during steady state and nonsteady state storage conditions. J Food Sci 47(1):92–96CrossRefGoogle Scholar
  105. 105.
    CGA D et al (1998) Indication of the Maillard reaction during storage of protein isolates. J Agric Food Chem 46(2):2485–2489Google Scholar
  106. 106.
    Morales FJ et al (1996) Fluorescence associated with Maillard reaction in milk and milk-resembling systems. Food Chem 57(3):423–428CrossRefGoogle Scholar
  107. 107.
    Suárez G et al (1995) Fructated protein is more resistant to ATP-dependent proteolysis than glucated protein possibly as a result of higher content of Maillard fluorophores. Arch Biochem Biophys 321(1):209–213PubMedCrossRefPubMedCentralGoogle Scholar
  108. 108.
    FJ M, MAJSvan B (1998) A study on advanced Maillard reaction in heated casein/sugar solutions: fluorescence accumulation. Int Dairy J 7(11):675–683Google Scholar
  109. 109.
    Yanagisawa K et al (1998) Specific fluorescence assay for advanced glycation end products in blood and urine of diabetic patients. Metab Clin Exp 47(11):1348–1353PubMedCrossRefPubMedCentralGoogle Scholar
  110. 110.
    VA Y et al (1992) A fluorescamine-based assay for the degree of glycation in bovine serum albumin. Food Res Int 25(4):269–275CrossRefGoogle Scholar
  111. 111.
    Uribarri J et al (2010) Advanced glycation end products in foods and a practical guide to their reduction in the diet. J Am Diet Assoc 110(6):911–916. e12PubMedPubMedCentralCrossRefGoogle Scholar
  112. 112.
    Dittrich R et al (2006) Concentrations of Nε-carboxymethyllysine in human breast milk, infant formulas, and urine of infants. J Agric Food Chem 54(18):6924PubMedCrossRefPubMedCentralGoogle Scholar
  113. 113.
    Šebeková K et al (2001) Plasma levels of advanced glycation end products in healthy, long-term vegetarians and subjects on a western mixed diet. Eur J Nutr 40(6):275–281PubMedCrossRefPubMedCentralGoogle Scholar
  114. 114.
    Miyazawa N et al (1998) Immunological detection of fructated proteins in vitro and in vivo. Biochem J 336. ( Pt 1(2):101PubMedPubMedCentralCrossRefGoogle Scholar
  115. 115.
    Mehta BM, Deeth HC (2016) Blocked lysine in dairy products: formation, occurrence, analysis, and nutritional implications. Compr Rev Food Sci Food Saf 15(1):206–218CrossRefGoogle Scholar
  116. 116.
    Krause R et al (2003) Studies on the formation of furosine and pyridosine during acid hydrolysis of different Amadori products of lysine. Eur Food Res Technol 216(4):277–283CrossRefGoogle Scholar
  117. 117.
    Nguyen HT et al (2014) N ϵ-(carboxymethyl)lysine: a review on analytical methods, formation, and occurrence in processed food, and health impact. Food Rev Int 30(1):36–52CrossRefGoogle Scholar
  118. 118.
    Charissou A et al (2007) Kinetics of formation of three indicators of the Maillard reaction in model cookies: influence of baking temperature and type of sugar. J Agric Food Chem 55(11):4532–4539PubMedCrossRefPubMedCentralGoogle Scholar
  119. 119.
    Tareke E et al (2013) Isotope dilution ESI-LC-MS/MS for quantification of free and total Nε-(1-Carboxymethyl)-l-Lysine and free Nε-(1-Carboxyethyl)-l-Lysine: Comparison of total Nε-(1-Carboxymethyl)-l-Lysine levels measured with new method to ELISA assay in gruel samples. Food Chem 141:4253–4259PubMedCrossRefPubMedCentralGoogle Scholar
  120. 120.
    Jiao Y et al (2017) N(epsilon)-(carboxymethyl)lysine and N(epsilon)-(carboxyethyl)lysine in tea and the factors affecting their formation. Food Chem 232:683–688PubMedCrossRefGoogle Scholar
  121. 121.
    Henle T, Klostermeyer H (1993) Determination of protein-bound 2-amino-6-(2-formyl-1-pyrrolyl). Z Lebensm Unters Forsch 196(1):1–4CrossRefGoogle Scholar
  122. 122.
    Schwarzenbolz U et al (2016) Free Maillard reaction products in milk reflect nutritional intake of glycated proteins and can be used to distinguish “organic” and “conventionally” produced milk. J Agric Food Chem 64(24):5071PubMedCrossRefGoogle Scholar
  123. 123.
    Hau J, Bovetto L (2001) Characterisation of modified whey protein in milk ingredients by liquid chromatography coupled to electrospray ionisation mass spectrometry. J Chromatogr A 926(1):105–112PubMedCrossRefGoogle Scholar
  124. 124.
    French SJ et al (2002) Maillard reaction induced lactose attachment to bovine beta-lactoglobulin: electrospray ionization and matrix-assisted laser desorption/ionization examination. J Agric Food Chem 50(4):820–823PubMedCrossRefGoogle Scholar
  125. 125.
    Akıllıoğlu HG et al (2017) Monitoring protein glycation by electrospray ionization (ESI) quadrupole time-of-flight (Q-TOF) mass spectrometer. Food Chem 217:65–73PubMedCrossRefGoogle Scholar
  126. 126.
    Meltretter J et al (2008) Identification and site-specific relative quantification of beta-lactoglobulin modifications in heated milk and dairy products. J Agric Food Chem 56(13):5165–5171PubMedCrossRefGoogle Scholar
  127. 127.
    Guerra PV, Yaylayan VA (2014) Interaction of flavanols with amino acids: postoxidative reactivity of the B-ring of catechin with glycine. J Agric Food Chem 62(17):3831–3836PubMedCrossRefGoogle Scholar
  128. 128.
    Yin J et al (2014) Epicatechin and epigallocatechin gallate inhibit formation of intermediary radicals during heating of lysine and glucose. Food Chem 146(1):C48–C55CrossRefGoogle Scholar
  129. 129.
    Sang S, Shao X, Bai N, Lo CY, Yang CS, Ho CT (2007) Tea Polyphenol (−)-epigallocatechin-3-gallate: A new trapping agent of reactive dicarbonyl species. Chem Res Toxicol 20:1862–1870PubMedCrossRefGoogle Scholar
  130. 130.
    Schilling S et al (2010) Characterization of covalent addition products of chlorogenic acid quinone with amino acid derivatives in model systems and apple juice by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun Mass Spectrom 22(4):441–448CrossRefGoogle Scholar
  131. 131.
    Wu CH et al (2011) Inhibition of advanced glycation end product formation by foodstuffs. Food Funct 2(5):224–234PubMedCrossRefPubMedCentralGoogle Scholar
  132. 132.
    Freedman BI et al (1999) Design and baseline characteristics for the aminoguanidine Clinical Trial in Overt Type 2 Diabetic Nephropathy (ACTION II). Control Clin Trials 20(5):493–510PubMedCrossRefPubMedCentralGoogle Scholar
  133. 133.
    Williams ME (2004) Clinical studies of advanced glycation end product inhibitors and diabetic kidney disease. Curr Diab Rep 4(6):441–446PubMedCrossRefPubMedCentralGoogle Scholar
  134. 134.
    Méndez JD, Leal LI (2004) Inhibition of in vitro pyrraline formation by L-arginine and polyamines. Biomed Pharmacother 58(10):598–604PubMedCrossRefPubMedCentralGoogle Scholar
  135. 135.
    Mendez JD, Balderas FL (2006) Inhibition by L-arginine and spermidine of hemoglobin glycation and lipid peroxidation in rats with induced diabetes. Biomed Pharmacother 60(1):26–31PubMedCrossRefPubMedCentralGoogle Scholar
  136. 136.
    Jafarnejad A et al (2008) Effect of spermine on lipid profile and HDL functionality in the streptozotocin-induced diabetic rat model. Life Sci 82(5):301–307PubMedCrossRefPubMedCentralGoogle Scholar
  137. 137.
    Kim J et al (2011) Chlorogenic acid inhibits the formation of advanced glycation end products and associated protein cross-linking. Arch Pharm Res 34(3):495–500PubMedCrossRefPubMedCentralGoogle Scholar
  138. 138.
    Kim YS et al (2011) Preventive effect of chlorogenic acid on lens opacity and cytotoxicity in human lens epithelial cells. Biol Pharm Bull 34(6):925–928PubMedCrossRefPubMedCentralGoogle Scholar
  139. 139.
    Gasser P et al (2011) Glycation induction and antiglycation activity of skin care ingredients on living human skin explants. Int J Cosmet Sci 33(4):366–370PubMedCrossRefPubMedCentralGoogle Scholar
  140. 140.
    Harris CS et al (2014) Investigating wild berries as a dietary approach to reducing the formation of advanced glycation end products: chemical correlates of in vitro antiglycation activity. Plant Foods Hum Nutr 69(1):71–77PubMedPubMedCentralCrossRefGoogle Scholar
  141. 141.
    Mesías M et al (2012) Antiglycative effect of fruit and vegetable seed extracts: inhibition of AGE formation and carbonyl-trapping abilities. J Sci Food Agric 93(8):2037–2044CrossRefGoogle Scholar
  142. 142.
    Sri Harsha PSC et al (2014) Protective ability of phenolics from white grape vinification by-products against structural damage of bovine serum albumin induced by glycation. Food Chem 156:220–226PubMedCrossRefPubMedCentralGoogle Scholar
  143. 143.
    Silván JM et al (2011) Control of the Maillard reaction by ferulic acid. Food Chem 128(1):208–213PubMedCrossRefPubMedCentralGoogle Scholar
  144. 144.
    Cömert ED et al (2017) Mitigation of ovalbumin glycation in vitro by its treatment with green tea polyphenols. Eur Food Res Technol 243(1):11–19CrossRefGoogle Scholar
  145. 145.
    Silvan JM et al (2014) Glycation is regulated by isoflavones. Food Funct 5(9):2036–2042PubMedCrossRefPubMedCentralGoogle Scholar
  146. 146.
    Fernandez-Gomez B et al (2015) New knowledge on the antiglycoxidative mechanism of chlorogenic acid. Food Funct 6(6):2081–2090PubMedCrossRefPubMedCentralGoogle Scholar
  147. 147.
    Akıllıoğlu HG, Gökmen V (2014) Effects of hydrophobic and ionic interactions on glycation of casein during Maillard reaction. J Agric Food Chem 62(46):11289–11295PubMedCrossRefPubMedCentralGoogle Scholar
  148. 148.
    Akıllıoğlu HG, Gökmen V (2016) Kinetic evaluation of the inhibition of protein glycation during heating. Food Chem 196:1117–1124PubMedCrossRefPubMedCentralGoogle Scholar
  149. 149.
    Moeckel U et al (2016) Glycation reactions of casein micelles. J Agric Food Chem 64(14):2953–2961PubMedCrossRefPubMedCentralGoogle Scholar
  150. 150.
    Peng X et al (2010) The effects of grape seed extract fortification on the antioxidant activity and quality attributes of bread. Food Chem 119(1):49–53CrossRefGoogle Scholar
  151. 151.
    Srey C et al (2010) Effect of inhibitor compounds on Nε-(Carboxymethyl)lysine (CML) and Nε-(Carboxyethyl)lysine (CEL) formation in model foods. J Agric Food Chem 58(22):12036–12041PubMedCrossRefPubMedCentralGoogle Scholar
  152. 152.
    Wang J et al (2009) Protein glycation inhibitory activity of wheat bran feruloyl oligosaccharides. Food Chem 112(2):350–353CrossRefGoogle Scholar
  153. 153.
    Zhang X et al (2014) Treatment of proteins with dietary polyphenols lowers the formation of AGEs and AGE-induced toxicity. Food Funct 5(10):2656–2661PubMedCrossRefGoogle Scholar
  154. 154.
    Zhang X et al (2014) Antioxidant and antiglycation activity of selected dietary polyphenols in a cookie model. J Agric Food Chem 62(7):1643–1648PubMedPubMedCentralCrossRefGoogle Scholar
  155. 155.
    Kong Y et al (2015) Glycation of β-lactoglobulin and antiglycation by genistein in different reactive carbonyl model systems. Food Chem 183:36–42PubMedCrossRefGoogle Scholar
  156. 156.
    Li X et al (2014) Quercetin inhibits advanced glycation end product formation by trapping methylglyoxal and glyoxal. J Agric Food Chem 62(50):12152–12158PubMedPubMedCentralCrossRefGoogle Scholar
  157. 157.
    Totlani VM, Peterson DG (2005) Reactivity of epicatechin in aqueous glycine and glucose maillard reaction models: quenching of C2, C3, and C4 sugar fragments. J Agric Food Chem 53(10):4130–4135PubMedCrossRefGoogle Scholar
  158. 158.
    Totlani VM, Peterson DG (2007) influence of epicatechin reactions on the mechanisms of Maillard product formation in low moisture model systems. J Agric Food Chem 55(2):414–420PubMedCrossRefGoogle Scholar
  159. 159.
    Totlani VM, Peterson DG (2006) Epicatechin carbonyl-trapping reactions in aqueous maillard systems: identification and structural elucidation. J Agric Food Chem 54(19):7311–7318PubMedCrossRefGoogle Scholar
  160. 160.
    Noda Y, Peterson DG (2007) Structure−reactivity relationships of flavan-3-ols on product generation in aqueous glucose/glycine model systems. J Agric Food Chem 55(9):3686–3691PubMedCrossRefGoogle Scholar
  161. 161.
    Bin Q et al (2012) Influence of phenolic compounds on the mechanisms of pyrazinium radical generation in the Maillard reaction. J Agric Food Chem 60(21):5482–5490PubMedCrossRefGoogle Scholar
  162. 162.
    Peng X et al (2011) Naturally occurring inhibitors against the formation of advanced glycation end-products. Food Funct 2(6):289–301PubMedCrossRefGoogle Scholar
  163. 163.
    Reddy VP, Beyaz A (2006) Inhibitors of the Maillard reaction and AGE breakers as therapeutics for multiple diseases. Drug Discov Today 11(13):646–654PubMedCrossRefGoogle Scholar
  164. 164.
    Kocadağlı T et al (2016) Formation of α-dicarbonyl compounds in cookies made from wheat, hull-less barley and colored corn and its relation with phenolic compounds, free amino acids and sugars. Eur Food Res Technol 242(1):51–60CrossRefGoogle Scholar
  165. 165.
    Hurrell RF, Finot P-A (1984) Nutritional consequences of the reactions between proteins and oxidized polyphenolic acids. In: Friedman M (ed) Nutritional and toxicological aspects of food safety. Springer, Boston, pp 423–435CrossRefGoogle Scholar
  166. 166.
    Rawel HM et al (2001) Reactions of phenolic substances with lysozyme — physicochemical characterisation and proteolytic digestion of the derivatives. Food Chem 72(1):59–71CrossRefGoogle Scholar
  167. 167.
    Ali H(2002) Protein-phenolic interactions in foodGoogle Scholar
  168. 168.
    Oh HI et al (1980) Hydrophobic interaction in tannin-protein complexes. J Agric Food Chem 28(2):394–398CrossRefGoogle Scholar
  169. 169.
    Vlassopoulos A et al (2014) Protein–phenolic interactions and inhibition of glycation–combining a systematic review and experimental models for enhanced physiological relevance. Food Funct 5(10):2646–2655PubMedCrossRefPubMedCentralGoogle Scholar
  170. 170.
    Xiao J, Kai G (2012) A review of dietary polyphenol-plasma protein interactions: characterization, influence on the bioactivity, and structure-affinity relationship. Crit Rev Food Sci Nutr 52(1):85–101PubMedCrossRefGoogle Scholar

Copyright information

© Springer Nature Singapore Pte Ltd. 2019

Authors and Affiliations

  1. 1.Department of Food Science, Faculty of ScienceUniversity of CopenhagenFrederiksbergDenmark
  2. 2.Food Quality and Safety (FoQuS) Research Group, Food Engineering DepartmentHacettepe UniversityAnkaraTurkey

Personalised recommendations