Конечные продукты гликирования и технологические аспекты снижения иммуногенности специализированных пищевых продуктов для питания спортсменов

Пищевая аллергия, которой страдают около 8% детей и 5% взрослых в мире, является одной из основных проблем мирового здравоохранения, а контроль аллергенов — важным аспектом безопасности пищевых продуктов. Согласно FALCPA (Food Allergen Labeling and Consumer Protection Act of 2004, FDA), более 160 продуктов питания могут вызывать аллергические реакции, при этом восемь из них ответственны за 90% всех случаев пищевой аллергии. К этим продуктам относятся молоко, яйцо, пшеница, арахис, соя, орех, ракообразные и рыба, также известные как «Большая восьмерка». Большинство пищевых продуктов, являющихся источником облигатных аллергенов, подвергается термической обработке перед употреблением. Это может вызывать инициацию реакции Майяра, в ходе которой образуются конечные продукты гликации. Известно, что симптомы пищевой сенсибилизации значительно влияют на качество жизни, разнообразие кишечного микробиома и адаптационный потенциал. В частности у спортсменов это может выражаться в снижении эффективности тренировочного процесса, что приводит к ухудшению показателей выносливости и спортивной производительности. В связи с этим представляется актуальным изучение влияния реакции Майяра и AGEs на иммуногенность белков и анализ возможной связи между этими соединениями и пищевой аллергией, а также разработка мероприятий по профилактике неблагоприятного воздействия аллергенов на организм профессионального спортсмена и любого другого потребителя.

1. Somoza, V., Wenzel, E., Weiß, C., Clawin-Rädecker, I., Grübel, N., Erbersdobler, H. F. (2006). Dose-dependent utilisation of casein-linked lysinoalanine, N(epsilon)-fructoselysine and N(epsilon)-carboxymethyllysine in rats. Molecular Nutrition and Food Research, 50(9), 833–841. https://doi.org/10.1002/mnfr.200600021

2. Hellwig, M., Henle, T. (2014). Baking, ageing, diabetes: A short history of the maillard reaction. Angewandte Chemie — International Edition, 53(39), 10316–10329. https://doi.org/10.1002/anie.201308808

3. de Oliveira, F. C., Coimbra, J. S. D. R., de Oliveira, E. B., Zuñiga, A. D. G., Rojas, E. E. G. (2016). Food protein-polysaccharide conjugates obtained via the Maillard reaction: A review. Critical Reviews in Food Science and Nutrition, 56(7), 1108–1125. https://doi.org/10.1080/10408398.2012.755669

4. Teodorowicz, M., Van Neerven, J., Savelkoul, H. (2017). Food processing: The influence of the Maillard reaction on immunogenicity and allergenicity of food proteins. Nutrients, 9(8), Article 835. https://doi.org/10.3390/nu9080835

5. Xiang, J., Liu, F., Wang, B., Chen, L., Liu, W., Tan, S. (2021). A literature review on Maillard reaction based on milk proteins and carbohydrates in food and pharmaceutical products: Advantages, disadvantages, and avoidance strategies. Foods, 10(9), Article 1998. https://doi.org/10.3390/foods10091998

6. Newton, A. E., Fairbanks, A. J., Golding, M., Andrewes, P., Gerrard, J. A. (2012). The role of the Maillard reaction in the formation of flavour compounds in dairy products — not only a deleterious reaction but also a rich source of flavour compounds. Food and Function, 3(12), 1231–1241. https://doi.org/10.1039/c2fo30089c

7. Nooshkam, M., Varidi, M., Bashash, M. (2019). The Maillard reaction products as food-born antioxidant and antibrowning agents in model and real food systems. Food Chemistry, 275, 644–660. https://doi.org/10.1016/j.foodchem.2018.09.083

8. Oliver, C. M., Melton, L. D., Stanley, R. A. (2006). Creating proteins with novel functionality via the maillard reaction: A review. Critical Reviews in Food Science and Nutrition, 46(4), 337–350. https://doi.org/10.1080/10408690590957250

9. Abd El-Salam, M. H., El-Shibiny, S. (2018). Glycation of whey proteins: Technological and nutritional implications. International Journal of Biological Macromolecules, 112, 83–92. https://doi.org/10.1016/j.ijbiomac.2018.01.114

10. Sedaghat Doost, A., Nikbakht Nasrabadi, M., Wu, J., A’yun, Q., Van der Meeren, P. (2019). Maillard conjugation as an approach to improve whey proteins functionality: A review of conventional and novel preparation techniques. Trends in Food Science and Technology, 91, 1–11. https://doi.org/10.1016/j.tifs.2019.06.011

11. Seo, C. W., Yoo, B. (2021). Preparation of milk protein isolate/κcarrageenan conjugates by Maillard reaction in wet-heating system and their application to stabilization of oil-in-water emulsions. LWT, 139, Article 110542. https://doi.org/10.1016/j.lwt.2020.110542

12. Meydani, B., Vahedifar, A., Askari, G., Madadlou, A. (2019). Influence of the Maillard reaction on the properties of cold-set whey protein and maltodextrin binary gels. International Dairy Journal, 90, 79–87. https://doi.org/10.1016/j.idairyj.2018.11.009

13. Andrade, M. A., Ribeiro-Santos, R., Guerra, M., Sanches-Silva, A. (2019). Evaluation of the oxidative status of salami packaged with an active whey protein film. Foods, 8(9), Article 387. https://doi.org/10.3390/foods8090387

14. Spanneberg, R., Salzwedel, G., Glomb, M. A. (2012). Formation of early and advanced Maillard reaction products correlates to the ripening of cheese. Journal of Agricultural and Food Chemistry, 60(2), 600–607. https://doi.org/10.1021/jf204079f

15. Erbersdobler, H. F., Somoza, V. (2007). Forty years of furosine — forty years of using Maillard reaction products as indicators of the nutritional quality of foods. Molecular Nutrition and Food Research, 51(4), 423–430. https://doi.org/10.1002/mnfr.200600154

16. García, M. M., Seiquer, I., Delgado-Andrade, C., Galdó, G., Navarro, M. P. (2009). Intake of Maillard reaction products reduces iron bioavailability in male adolescents. Molecular Nutrition and Food Research, 53(12), 1551–1560. https://doi.org/10.1002/mnfr.200800330

17. ALjahdali, N., Carbonero, F. (2019). Impact of Maillard reaction products on nutrition and health: Current knowledge and need to understand their fate in the human digestive system. Critical Reviews in Food Science and Nutrition, 59(3), 474–487. https://doi.org/10.1080/10408398.2017.1378865

18. Wang, Z., Jiang, Y., Liu, N., Ren, L., Zhu, Y., An, Y. et al. (2012). Advanced glycation end-product N e{open}- carboxymethyl-lysine accelerates progression of atherosclerotic calcification in diabetes. Atherosclerosis, 221(2), 387–396. https://doi.org/10.1016/j.atherosclerosis.2012.01.019

19. Li, J., Liu, D., Sun, L., Lu, Y., Zhang, Z. (2012). Advanced glycation end products and neurodegenerative diseases: Mechanisms and perspective. Journal of the Neurological Sciences, 317(1–2), 1–5. https://doi.org/10.1016/j.jns.2012.02.018

20. Rao, Q., Jiang, X., Li, Y., Samiwala, M., Labuza, T. P. (2018). Can glycation reduce food allergenicity? Journal of Agricultural and Food Chemistry, 66(17), 4295–4299. https://doi.org/10.1021/acs.jafc.8b00660

21. Yang, S. -Y., Kim, S. -W., Kim, Y., Lee, S. -H., Jeon, H., Lee, K. -W. (2015). Optimization of Maillard reaction with ribose for enhancing anti-allergy effect of fish protein hydrolysates using response surface methodology. Food Chemistry, 176, 420–425. https://doi.org/10.1016/j.foodchem.2014.12.090

22. Liu, E. G., Yin, X., Swaminathan, A., Eisenbarth, S. C. (2021). Antigenpresenting cells in food tolerance and allergy. Frontiers in Immunology, 11, Article 616020. https://doi.org/10.3389/fimmu.2020.616020

23. Bøgh, K. L., Madsen, C. B. (2016). Food allergens: Is there a correlation between stability to digestion and allergenicity? Critical Reviews in Food Science and Nutrition, 56(9), 1545–1567. https://doi.org/10.1080/10408398.2013.779569

24. Teodorowicz, M., Hendriks, W. H., Wichers, H. J., Savelkoul, H. F. J. (2018). Immunomodulation by processed animal feed: The role of maillard reaction products and advanced glycation end-products (AGEs). Frontiers in Immunology, 9(SEP), Article 2088. https://doi.org/10.3389/fimmu.2018.02088

25. Bastos, D. H. M., Gugliucci, A. (2015). Contemporary and controversial aspects of the Maillard reaction products. Current Opinion in Food Science, 1(1), 13–20. https://doi.org/10.1016/j.cofs.2014.08.001

26. Sanz, M. L., Corzo-Martínez, M., Rastall, R. A., Olano, A., Moreno, F. J. (2007). Characterization and in vitro digestibility of bovine β-lactoglobulin glycated with galactooligosaccharides. Journal of Agricultural and Food Chemistry, 55(19), 7916–7925. https://doi.org/10.1021/jf071111l

27. Zhang, Z., Li, Z., Lin, H. (2021). Reducing the allergenicity of shrimp tropomyosin and allergy desensitization based on glycation modification. Journal of Agricultural and Food Chemistry. https://doi.org/10.1021/acs.jafc.1c03953 (unpublished data)

28. Xu, L., Gong, Y., Gern, J. E., Ikeda, S., Lucey, J. A. (2018). Glycation of whey protein with dextrans of different molar mass: Effect on immunoglobulin E-binding capacity with blood sera obtained from patients with cow milk protein allergy. Journal of Dairy Science, 101(8), 6823–6834. https://doi.org/10.3168/jds.2017–14338

29. Maleki, S. J., Chung, S. -Y., Champagne, E. T., Raufman, J. -P. (2000). The effects of roasting on the allergenic properties of peanut proteins. Journal of Allergy and Clinical Immunology, 106(4), 763–768. https://doi.org/10.1067/mai.2000.109620

30. Liu, F., Teodorowicz, M., Van Boekel, M. A. J. S., Wichers, H. J., Hettinga, K. A. (2016). The decrease in the IgG-binding capacity of intensively dry heated whey proteins is associated with intense Maillard reaction, structural changes of the proteins and formation of RAGE-ligands. Food and Function, 7(1), 239–249. https://doi.org/10.1039/c5fo00718f

31. De Martinis, M., Sirufo, M. M., Suppa, M., Ginaldi, L. (2020). New perspectives in food allergy. International Journal of Molecular Sciences, 21(4), Article 1474. https://doi.org/10.3390/ijms21041474

32. Gupta, R. K., Gupta, K., Sharma, A., Das, M., Ansari, I. A., Dwivedi, P. D. (2018). Maillard reaction in food allergy: Pros and cons. Critical Reviews in Food Science and Nutrition, 58(2), 208–226. https://doi.org/10.1080/10408398.2016.1152949

33. Liang, Z., Chen, X., Li, L., Li, B., Yang, Z. (2019). The fate of dietary advanced glycation end products in the body: From oral intake to excretion. Critical Reviews in Food Science and Nutrition, 60(20), 3475–3491. https://doi.org/10.1080/10408398.2019.1693958

34. Hegele, J., Buetler, T., Delatour, T. (2008). Comparative LC–MS/MS profiling of free and protein-bound early and advanced glycation-induced lysine modifications in dairy products. Analytica Chimica Acta, 617(1–2), 85–96. https://doi.org/10.1016/j.aca.2007.12.027

35. Ling, B., Tang, J., Kong, F., Mitcham, E. J., Wang, S. (2015). Kinetics of food quality changes during thermal processing: A review. Food and Bioprocess Technology, 8(2), 343–358. https://doi.org/10.1007/s11947–014–1398–3

36. Collin, M., Bigley, V. (2018). Human dendritic cell subsets: An update. Immunology, 154(1), 3–20 https://doi.org/10.1111/imm.12888

37. Jaiswal, N., Agrawal, S., Agrawal, A. (2019). High fructose-induced metabolic changes enhance inflammation in human dendritic cells. Clinical and Experimental Immunology, 197(2), 237–249. https://doi.org/10.1111/cei.13299

38. Uribarri, J., Woodruff, S., Goodman, S., Cai, W., Chen, X., Pyzik, R. et al. (2010). Advanced glycation end products in foods and a practical guide to their reduction in the diet. Journal of the American Dietetic Association, 110(6), 911–916.e12. https://doi.org/10.1016/j.jada.2010.03.018

39. Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., Simm, A. (2014). Role of advanced glycation end products in cellular signaling. Redox Biology, 2(1), 411–429. https://doi.org/10.1016/j.redox.2013.12.016

40. Saleh, A., Smith, D. R., Tessler, L., Mateo, A. R., Martens, C., Schartner, E. et al. (2013). Receptor for advanced glycation end-products (RAGE) activates divergent signaling pathways to augment neurite outgrowth of adult sensory neurons. Experimental Neurology, 249, 149–159. https://doi.org/10.1016/j.expneurol.2013.08.018

41. Cai, W., Ramdas, M., Zhu, L., Chen, X., Striker, G. E., Vlassara, H. (2012). Oral advanced glycation endproducts (AGEs) promote insulin resistance and diabetes by depleting the antioxidant defenses AGE receptor-1 and sirtuin 1. Proceedings of the National Academy of Sciencesof the United States of America, 109(39), 15888–15893. https://doi.org/10.1073/pnas.1205847109

42. Ilchmann, A., Burgdorf, S., Scheurer, S., Waibler, Z., Nagai, R., Wellner, A. et al. (2010). Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: Role of macrophage scavenger receptor class A type I and II. The Journal of Allergy and Clinical Immunology, 125(1–3), 175–183.e11. https://doi.org/10.1016/j.jaci.2009.08.013

43. Maillard-Lefebvre, H., Boulanger, E., Daroux, M., Gaxatte, C., Hudson, B. I., Lambert, M. (2009). Soluble receptor for advanced glycation end products: A new biomarker in diagnosis and prognosis of chronic inflammatory diseases. Rheumatology (Oxford, England), 48(10), 1190–1196. https://doi.org/10.1093/rheumatology/kep199

44. Jiménez-Saiz, R., Belloque, J., Molina, E., López-Fandiño, R. (2011). Human immunoglobulin e (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. Journal of Agricultural and Food Chemistry, 59(18), 10044–10051https://doi.org/10.1021/jf2014638

45. Taheri-Kafrani, A., Gaudin, J.-C., Rabesona, H., Nioi, C., Agarwal, D., Drouet, M. et al. (2009). Effects of heating and glycation of β-lactoglobulin on its recognition by ige of sera from cow milk allergy patients. Journal of Agricultural and Food Chemistry, 57(11), 4974–4982. https://doi.org/10.1021/jf804038t

46. Bu, G., Lu, J., Zheng, Z., Luo, Y. (2009). Influence of maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methsodology. Journal of the Science of Food and Agriculture, 89(14), 2428–2434. https://doi.org/10.1002/jsfa.3741

47. Heilmann, M., Wellner, A., Gadermaier, G., Ilchmann, A., Briza, P., Krause, M. et al. (2014). Ovalbumin modified with pyrraline, a maillard reaction product, shows enhanced T-cell immunogenicity. Journal of Biological Chemistry, 289(11), 7919–7928. https://doi.org/10.1074/jbc.M113.523621

48. Cucu, T., De Meulenaer, B., Bridts, C., Devreese, B., Ebo, D. (2012). Impact of thermal processing and the maillard reaction on the basophil activation of hazelnut allergic patients. Food and Chemical Toxicology, 50(5), 1722–1728. https://doi.org/10.1016/j.fct.2012.02.069

49. Han, X.-Y., Yang, H., Rao, S.-T., Liu, G.-Y., Hu, M.-J., Zeng, B.-C. et al. (2018). The Maillard reaction reduced the sensitization of tropomyosin and arginine kinase from Scylla paramamosain, simultaneously. Journal of Agricultural and Food Chemistry, 66(11), 2934–2943. https://doi.org/10.1021/acs.jafc.7b05195

50. Zhang, Z., Li, X. -M., Xiao, H., Nowak-Wegrzyn, A., Zhou, P. (2020). Insight into the allergenicity of shrimp tropomyosin glycated by functional oligosaccharides containing advanced glycation end products. Food Chemistry, 302, Article 125348. https://doi.org/10.1016/j.foodchem.2019.125348

51. Zhao, Y.-J., Cai, Q.-F., Jin, T., Zhang, L.-J., Fei, D.-X., Liu, G.-M., Cao, M.-J. (2017). Effect of Maillard reaction on the structural and immunological properties of recombinant silver carp parvalbumin. LWT — Food Science and Technology, 75, 25–33. https://doi.org/10.1016/j.lwt.2016.08.049

52. Kobelkova, M.S., Korosteleva, M.M., Kobelkova, I.V. (2021). Applied aspects of the use of Maillard reaction products in the development of specialized food products for the nutrition of athletes. Food systems, 4(3S), 137–141. https://doi.org/10.21323/2618–9771–2021–4–3S-137–141

53. Yang, Z. -H., Li, C., Li, Y. -Y., Wang, Z. -H. (2013). Effects of maillard reaction on allergenicity of buckwheat allergen fag t 3 during thermal processing. Journal of the Science of Food and Agriculture, 93(6), 1510–1515. https://doi.org/10.1002/jsfa.5928

54. Warren, C.M., Jiang, J., Gupta, R.S. (2020). Epidemiology and burden of food allergy. Current Allergy and Asthma Reports, 20(2), Article 6. https://doi.org/10.1007/s11882–020–0898–7

55. Warren, C. M., Turner, P. J., Chinthrajah, R. S., Gupta, R. S. (2021). Advancing food allergy through epidemiology: Understanding and addressing disparities in food allergy management and outcomes. Journal of Allergy and Clinical Immunology: In Practice, 9(1), 110–118. https://doi.org/10.1016/j.jaip.2020.09.064

56. Smith, P. K., Masilamani, M., Li, X. -M., Sampson, H. A. (2017). The false alarm hypothesis: Food allergy is associated with high dietary advanced glycation end-products and proglycating dietary sugars that mimic alarmins. Journal of Allergy and Clinical Immunology, 139(2), 429–437. https://doi.org/10.1016/j.jaci.2016.05.040

57. Wei, Q., Liu, T., Sun, D. -W. (2018). Advanced glycation end-products (AGEs) in foods and their detecting techniques and methods: A review. Trends in Food Science and Technology, 82, 32–45. https://doi.org/10.1016/j.tifs.2018.09.020

58. Takeuchi, M., Takino, J., Furuno, S., Shirai, H., Kawakami, M., Muramatsu, M. et al. (2015). Assessment of the concentrations of various advanced glycation end-products in beverages and foods that are commonly consumed in Japan. Plos One, 10(3), Article e0118652. https://doi.org/10.1371/journal.pone.0118652

59. Hull, G. L. J., Woodside, J. V., Ames, J. M., Cuskelly, G. J. (2012). N ε (carboxymethyl) lysine content of foods commonly consumed in a Western style diet. Food Chemistry, 131(1), 170–174. https://doi.org/10.1016/j.foodchem.2011.08.055

60. Pouillart, P., Mauprivez, H., Ait-Ameur, L., Cayzeele, A., Lecerf, J., Tessier, F. J. et al. (2008). Strategy for the study of the health impact of dietary Maillard products in clinical studies: The example of the ICARE clinical study on healthy adults. Annals of the New York Academy of Sciences, 1126, 173–176. https://doi.org/10.1196/annals.1433.040

61. Zhang, Z., Li, D. (2018). Thermal processing of food reduces gut microbiota diversity of the host and triggers adaptation of the microbiota: Evidence from two vertebrates. Microbiome, 6(1), 99. https://doi.org/10.1186/s40168–018–0471-y

62. Koliada, A., Syzenko, G., Moseiko, V., Budovska, L., Puchkov, K., Perederiy, V. et al. (2017). Association between body mass index and Firmicutes/ Bacteroidetes ratio in an adult Ukrainian population. BMC Microbiology, 17(1), Article 120. https://doi.org/10.1186/s12866–017–1027–1

63. Mao, Z., Ren, Y., Zhang, Q., Dong, S., Han, K., Feng, G. et al. (2019). Glycated fish protein supplementation modulated gut microbiota composition and reduced inflammation but increased accumulation of advanced glycation end products in high-fat diet fed rats. Food and Function, 10(6), 3439–3451. https://doi.org/10.1039/c9fo00599d

64. Yacoub, R., Nugent, M., Cai, W., Nadkarni, G. N., Chaves, L. D., Abyad, S. et al. (2017). Advanced glycation end products dietary restriction effects on bacterial gut microbiota in peritoneal dialysis patients; a randomized open label controlled trial. PLoS One, 12(9), Article e0184789. https://doi.org/10.1371/journal.pone.0184789

65. Seiquer, I., Rubio, L. A., Peinado, M. J., Delgado-Andrade, C., Navarro, M. P. (2014). Maillard reaction products modulate gut microbiota composition in adolescents. Molecular Nutrition and Food Research, 58(7), 1552-1560. https://doi.org/10.1002/mnfr.201300847

66. Luévano-Contreras, C., Garay-Sevilla, M. E., Wrobel, K., Malacara, J. M., Wrobel, K. (2012). Dietary advanced glycation end products restriction diminishes inflammation markers and oxidative stress in patients with type 2 diabetes mellitus. Journal of Clinical Biochemistry and Nutrition, 52(1), 12–40. https://doi.org/10.3164/jcbn.12–40

67. Vlassara, H., Striker, G. E. (2011). AGE restriction in diabetes mellitus: A paradigm shift. Nature Reviews Endocrinology, 7(9), 526–539. https://doi.org/10.1038/nrendo.2011.74

68. Di Pino, A., Currenti, W., Urbano, F., Mantegna, C., Purrazzo, G., Piro, S. et al. (2016). Low advanced glycation end product diet improves the lipid and inflammatory profiles of prediabetic subjects. Journal of Clinical Lipidology, 10(5), 1098–1108. https://doi.org/10.1016/j.jacl.2016.07.001

69. Poulsen, M. W., Bak, M. J., Andersen, J. M., Monošík, R., Giraudi-Futin, A. C., Holst, J. J. et al. (2014). Effect of dietary advanced glycation end products on postprandial appetite, inflammation, and endothelial activation in healthy overweight individuals. European Journal of Nutrition, 53(2), 661–672. https://doi.org/10.1007/s00394–013–0574-y

70. Macías-Cervantes, M. H., Rodríguez-Soto, J. M. D., Uribarri, J., DíazCisneros, F. J., Cai, W., Garay-Sevilla, M. E. (2015). Effect of an advanced glycation end product-restricted diet and exercise on metabolic parameters in adult overweight men. Nutrition, 31(3), 446–451. https://doi.org/10.1016/j.nut.2014.10.004

71. Munekata, P.E.S., Domínguez, R., Budaraju, S., Roselló-Soto, E., Barba, F.J., Mallikarjunan, K. et al. (2020). Effect of innovative food processing technologies on the physicochemical and nutritional properties and quality of non-dairy plant-based beverages. Foods, 9(3), Article 288. https://doi.org/10.3390/foods9030288

72. Khan, M., Liu, H., Wang, J., Sun, B. (2019). Inhibitory effect of phenolic compounds and plant extracts on the formation of advance glycation end products: A comprehensive review. Food Research International, 130, Article 108933. https://doi.org/10.1016/j.foodres.2019.108933

73. Abdallah, H. M., El-Bassossy, H., Mohamed, G. A., El-Halawany, A. M., Alshali, K. Z., Banjar, Z. M. (2016). Phenolics from Garcinia mangostana inhibit advanced glycation endproducts formation: Effect on amadori products, cross-linked structures and protein thiols. Molecules, 21(2), Article 251. https://doi.org/10.3390/molecules21020251

74. Zhu, R., Wang, C., Zhang, L., Wang, Y., Chen, G., Fan, J. et al. (2019). Pectin oligosaccharides from fruit of Actinidia arguta: Structure-activity relationship of prebiotic and antiglycation potentials. Carbohydrate Polymers, 217, 90–97. https://doi.org/10.1016/j.carbpol.2019.04.032

75. Sharma, C., Kaur, A., Thind, S. S., Singh, B., Raina, S. (2015). Advanced glycation end-products (AGEs): an emerging concern for processed food industries. Journal of Food Science and Technology, 52(12), 7561–7576. https://doi.org/10.1007/s13197–015–1851-y

76. Zhang, Q., Wang, Y., Fu, L. (2020). Dietary advanced glycation end-products: Perspectives linking food processing with health implications. Comprehensive Reviews in Food Science and Food Safety, 19(5), 559–2587. https://doi.org/10.1111/1541–4337.12593