Modulation of Maillard reaction and protein aggregation in bovine meat following exposure to microwave heating and possible impact on digestive processes: An FTIR spectroscopy study

References

• Akahane, T., S. Chihara, T. P. Niki, T. Sano, T. Tsuchiya, S. F. Noguchi, H. Ookami, and J. J. Matsumoto. 1985. Differential scanning calorimetric studies on thermal behaviour of myofibrillar proteins. Bull. Jap. Soc. Sci. Fish 51:1841–46. doi:10.2331/suisan.51.1841.
   Google Scholar
• Albi, T., A. Lanzon, A. Guinda, M. C. Pérez-Camino, and M. León. 1997. Microwave and conventional heating effects on some physical and chemical parameters of edible fats. J. Agric. Food Chem. 45:3000–03. doi:10.1021/jf970168c.
   Web of Science ®Google Scholar
• Al-Saidi, G. S., A. Al-Alawi, M. S. Rahman, and N. Guizani. 2012. Fourier Transform Infrared (FTIR) spectroscopic study of extracted gelatin from Shaari (Lithrinus microdon) skin: Effects of extraction conditions. Int. Food Res. J. 19:1167–73.
   Google Scholar
• Bastos, D. M., E. Monaro, E. Siguemoto, and M. Séfora. 2012. Maillard reaction products in processed food: Pros and Cons, food industrial processes - Methods and equipment. Benjamin Valdez (Ed.). Rijeka, Croatia: IntechOpen.
   Google Scholar
• Calabrò, E., S. Condello, M. Currò, N. Ferlazzo, M. Vecchio, D. Caccamo, S. Magazù, and R. Ientile. 2013. 50 Hz electromagnetic field produced changes in FTIR spectroscopy associated with mitochondrial transmembrane potential reduction in neuronal-like SH-SY5Y cells. Oxid. Med. Cell Longev. 2013:8. ID 414393. doi:10.1155/2013/414393.
   Web of Science ®Google Scholar
• Calabrò, E., and S. Magazù. 2012. Electromagnetic fields effects on the secondary structure of lysozyme and bioprotective effectiveness of trehalose. Adv. Phys. Chem. 2012:6. ID 970369. doi:10.1155/2012/970369.
   Google Scholar
• Calabrò, E., and S. Magazù. 2013a. Demicellization of polyethylene oxide in water solution under static magnetic field exposure studied by FTIR spectroscopy. Adv. Phys. Chem. 2013:8. ID 485865. doi:10.1155/2013/485865.
   Google Scholar
• Calabrò, E., and S. Magazù. 2013b. Unfolding and aggregation of myoglobin can be induced by three hours exposure to mobile phone microwaves: A FTIR spectroscopy study. Spectrosc. Lett. 46:583–89. doi:10.1080/00387010.2013.771274.
   Web of Science ®Google Scholar
• Calabrò, E., and S. Magazù. 2014a. Unfolding-induced in haemoglobin by exposure to electromagnetic fields: A FTIR spectroscopy study. Orient. J. Chem. 30:31–35. doi:10.13005/ojc.
   Google Scholar
• Calabrò, E., and S. Magazù. 2014b. Non-thermal effects of microwave oven heating on ground beef meat studied in the mid-infrared region by FTIR spectroscopy. Spectrosc. Lett. 47:649–56. doi:10.1080/00387010.2013.828313.
   Web of Science ®Google Scholar
• Calabrò, E., and S. Magazù. 2015. Fourier–self –deconvolution analysis of β-sheet contents in the Amide I region of haemoglobin aqueous solutions under exposure to 900 MHz microwaves and bioprotective effectiveness of sugars and salt solutions. Spectrosc. Lett. 48:741–47. doi:10.1080/00387010.2015.1011278.
   Web of Science ®Google Scholar
• Calabrò, E., and S. Magazù. 2016. Parallel β-sheet vibration band increases with proteins dipole moment under exposure to 1765 MHz microwaves. Bioelectromagnetics 37:99–107. doi:10.1002/bem.v37.2.
   PubMed Web of Science ®Google Scholar
• Calabrò, E., and S. Magazù. 2017a. The α-helix alignment of proteins in water solution towards a high frequency electromagnetic field: A FTIR spectroscopy study. Electromagn. Biol. Med. 36:279–88. doi:10.1080/15368378.2017.1328691.
   PubMed Web of Science ®Google Scholar
• Calabrò, E., and S. Magazù. 2017b. Effects of the addition of sodium chloride to a tetrameric protein in water solution during exposure to high frequency electromagnetic field. Open Biotechnol. J. 11:72–80. doi:10.2174/1874070701711010072.
   Google Scholar
• Calabrò, E., and S. Magazù. 2018. Direct spectroscopic evidence for competition between thermal molecular agitation and magnetic field in a tetrameric protein in aqueous solution. Phys. Lett. A 382:1389–94. doi:10.1016/j.physleta.2018.03.038.
   Web of Science ®Google Scholar
• Calabrò, E., S. Magazù, and S. Campo. 2012. Microwave-induced increase of Amide I and Amide II vibration bands and modulating functions of sodium-chloride, sucrose and trehalose aqueous solutions: The case study of haemoglobin. Res. J. Chem. Environ. 16:59–67.
   Web of Science ®Google Scholar
• Dumas, P., and L. Miller. 2003. The use of synchrotron infrared microspectroscopy in biological and biomedical investigations. Vib. Spectrosc. 32:3–21. doi:10.1016/S0924-2031(03)00043-2.
   Web of Science ®Google Scholar
• Dyson, H. J., and P. E. Wright. 1990. Peptide conformation and protein folding. Curr. Opin. Struct. Biol. 3:60–65. doi:10.1016/0959-440X(93)90203-W.
   Web of Science ®Google Scholar
• Fabian, H., and H. Mäntele. 2002. Infrared spectroscopy of proteins. In Handbook of vibrational spectroscopy, ed. J. M. Chalmers and P. R. Griffiths, 3399–425. Chichester: John Wiley & Sons Ltd.
   Google Scholar
• Fulton, L., and C. Davis. 1983. Roasting and braising beef roasts in microwave ovens. J. Am. Diet. Assoc. 83:560.
   PubMed Web of Science ®Google Scholar
• Gomaa, A. I., J. Sedman, and A. A. Ismail. 2013. An investigation of the effect of microwave treatment on the structure and unfolding pathways of beta-lactoglobulin using FTIR spectroscopy with the application of two-dimensional correlation spectroscopy (2D-COS). Vib. Spectrosc. 65:101–09. doi:10.1016/j.vibspec.2012.11.019.
   Web of Science ®Google Scholar
• Haque, E., B. R. Bhandari, M. J. Gidley, H. C. Deeth, S. M. Møller, and A. K. Whittaker. 2010. Protein conformational modifications and kinetics of water-protein interactions in milk protein concentrate powder upon aging: Effect on solubility. J. Agric. Food Chem. 58:7748–55. doi:10.1021/jf1007055.
   PubMed Web of Science ®Google Scholar
• Heddleson, R. A., and S. Doores. 1994. Factors affecting microwave heating of foods and microwave induced destruction of foodborne pathogens - A review. J. Food Prot. 57:1025–37. doi:10.4315/0362-028X-57.11.1025.
   PubMed Web of Science ®Google Scholar
• Hendriks, W. H., C. A. Butts, D. V. Thomas, K. A. C. James, P. C. A. Morel, and M. W. A. Verstegen. 2002. Nutritional quality and variation of meat and bone meal. Asian-Australas. J. Anim. Sci. 15:1507–16. doi:10.5713/ajas.2002.1507.
   Web of Science ®Google Scholar
• Herzallah, M. S. 2005. Influence of microwaving and conventional heating of milk on cholesterol contents and cholesterol oxides formation. Pak. J. Nutr. 4:85–88. doi:10.3923/pjn.2005.85.88.
   Google Scholar
• Hodge, J. E. 1953. Dehydrated foods. Chemistry of browning reaction in model systems. J. Agric. Food Chem. 1:928–43. doi:10.1021/jf60015a004.
   Web of Science ®Google Scholar
• Jackson, M., and H. H. Mantsch. 1995. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:95–120. doi:10.3109/10409239509085140.
   PubMed Web of Science ®Google Scholar
• Jeremiah, L. E., and L. L. Gibson. 2003. Cooking influences on the palatability of roasts from the beef hip. Food Resour. Int. 36:1–9. doi:10.1016/S0963-9969(02)00093-5.
   Web of Science ®Google Scholar
• Kong, J., and S. Yu. 2007. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim. Biophys. Sin. 39:549–59. doi:10.1111/j.1745-7270.2007.00320.x.
   Google Scholar
• Kumar, M., and B. D. Sharma. 2004. The storage stability and textural, physico-chemical, and sensory quality of low-fat ground pork patties with carrageenan as fat replacer. Int. J. Food Sci.Technol. 39:31–42. doi:10.1111/ifs.2004.39.issue-1.
   Web of Science ®Google Scholar
• Labuza, T. P. 1994. Interpreting the complexity of kinetics of the Maillard reaction. In The Maillard reaction in food, nutrition and health, ed. T. P. Labuza, G. A. Reineccuis, J. Baynes, and V. Monnier, 176–181. London, UK: Royal Society of Chemistry.
   Google Scholar
• Lund, M. N., and C. A. Ray. 2017. Control of Maillard reactions in foods: Strategies and chemical mechanisms. J. Agric. Food Chem. 65:4537−4552. doi:10.1021/acs.jafc.7b00882.
   PubMed Web of Science ®Google Scholar
• Maillard, L. C. 1912. Action des acides aminés sur les sucres; formation des mélanoidines par voie methodique. Comput. Rend. 154:66.
   Google Scholar
• Malheiro, R., I. Oliveira, and M. Vilas-Boas. 2009. Effect of microwave heating with different exposure times on physical and chemical parameters of olive oil. Food Chem. Toxicol 47:92–97. doi:10.1016/j.fct.2008.10.014.
   PubMed Web of Science ®Google Scholar
• Martins, S. I. F. S., W. M. F. Jongen, and M. A. J. S. van Boekel. 2001. A review of Maillard reaction in food and implications to kinetic modeling. Trends Food Sci.Technol. 11:364–73. doi:10.1016/S0924-2244(01)00022-X.
   Web of Science ®Google Scholar
• Matiacevich, S. B., P. R. Santagapita, and M. Pilar Buera. 2005. Fluorescence from the Maillard reaction and its potential applications in food science. Crit. Rev. Food Sci. Nutr. 45:483–95. doi:10.1080/10408390591034472.
   PubMed Web of Science ®Google Scholar
• Mauerer, A., and G. Lee. 2006. Changes in the amide IFT-IR bands of poly-L-lysine on spray-drying from alpha-helix, beta-sheet or random coil conformations. Eur. J. Pharm. Biopharm. 62:131–42. doi:10.1016/j.ejpb.2005.08.005.
   PubMed Web of Science ®Google Scholar
• Mingos, D. M. P., and D. R. Baghurst. 1997. Application of microwave dielectric heating effects to synthetic problems in chemistry. In Microwave-enhanced chemistry. Fundamentals, sample preparation, and applications, ed. H. M. Kingston and S. J. Haswell, 3–53. Washington, DC: American Chemists Society.
   Google Scholar
• Muhoza, B., S. Xia, J. Cai, X. Zhang, J. Su, and L. Li. 2017. Time effect on coenzyme Q10 loading and stability of micelles based on glycosylated casein via Maillard reaction. Food Hydrocoll. 72:271–80. doi:10.1016/j.foodhyd.2017.05.046.
   Web of Science ®Google Scholar
• Nagaraj, R. H., I. N. Shipanova, and F. M. Faust. 1996. Protein cross-linking by the Maillard reaction. J. Biol. Chem. 271:19338–45. doi:10.1074/jbc.271.32.19338.
   PubMed Web of Science ®Google Scholar
• Namiki, M. 1988. Chemistry of Maillard reactions: Recent studies on the browning reaction mechanism and the development of antioxidants and mutagens. Adv. Food Res. 32:115–84.
   PubMedGoogle Scholar
• Ohlsson, T. 1993. Domestic use of microwave ovens. In Encyclopaedia of food science food technology and nutrition, ed. R. Macrae, R. K. Robinson, and M. J. Sadler, vol. 2, 1232–37. London: Academic Press.
   Google Scholar
• Olinger, J. M., and P. R. Griffiths. 1993. Effects of sample dilution and particle size/morphology on diffuse reflection spectra of carbohydrate systems in the near- and mid-infrared. Part 1: Single analytes. Appl. Spectrosc. 47:687–94. doi:10.1366/0003702934066965.
   Web of Science ®Google Scholar
• Pawar, V. D., F. A. Khan, and B. S. Agarkar. 2002. Effect of fat/whey protein concentrate levels and cooking methods on textural characteristics of chevon patties. J. Food Sci. Technol. 39:429–31.
   Web of Science ®Google Scholar
• Powell, T. H., M. E. Dikeman, and M. C. Hunt. 2000. Tenderness and collagen composition of beef semitendinosus roasts cooked by conventional convective cooking and modeled, multi-stage, convective cooking. Meat Sci. 55:421–25. doi:10.1016/S0309-1740(99)00171-0.
   PubMed Web of Science ®Google Scholar
• Sanghoon, K. O., Y. O. O. Sang-Ho, L. E. E. Suyong, K.-H. Kim, and R. Hwang. 2011. Effect of long low temperature-short high temperature cooking cycle on physicochemical properties of beef. Food Sci. Technol. Resour. 17:11–16.
   Web of Science ®Google Scholar
• Santarelli, R. L., J.-L. Vendeuvre, N. Naud, S. Tache, F. Gueraud, M. Viau, C. Genot, D. E. Corpet, and F. H. F. Pierre. 2010. Meat processing and colon carcinogenesis: Cooked, nitrite-treated, and oxidized high-heme cured meat promotes mucin-depleted foci in rats. Cancer Prev. Res. 3:852–64. doi:10.1158/1940-6207.CAPR-09-0160.
   PubMed Web of Science ®Google Scholar
• Stabursvik, E., K. Fretheim, and T. Froystein. 1984. Myosin denaturation in pale, soft, and exudative (PSE) porcine muscle tissue as studied by differential scanning calorimetry. J. Sci. Food Agric. 35:240–44. doi:10.1002/()1097-0010.
   PubMed Web of Science ®Google Scholar
• Stuart, B. 2004. Infrared spectroscopy: Fundamentals and applications. Ed.. Toronto, Canada: John Wiley & Sons, Ltd.
   Google Scholar
• Tornberg, E. 2005. Effects of heat on meat proteins—Implications on structure and quality of meat products. Meat Sci. 70:493–508. doi:10.1016/j.meatsci.2004.11.021.
   PubMed Web of Science ®Google Scholar
• Van de Voort, F. R. 1992. Fourier transform infrared spectroscopy applied to food analysis. Food Resour. Int. 25:397–403. doi:10.1016/0963-9969(92)90115-L.
   Web of Science ®Google Scholar
• Wang, Y., R. I. Boysen, B. R. Wood, M. Kansiz, D. McNaughton, and M. T. W. Hearn. 2008. Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regression. Biopolymers 89:895–905. doi:10.1002/bip.v89:11.
   PubMed Web of Science ®Google Scholar
• Xiong, Y. L., C. J. Brekke, and H. K. Leung. 1987. Thermal denaturation of muscle proteins from different species and muscle types as studied by differential scanning calorimetry. Can. Inst. Food Sci. Technol. J. 20:357–62. doi:10.1016/S0315-5463(87)71331-5.
   Web of Science ®Google Scholar
• Yoshida, H., and G. Kajimoto. 1994. Microwave heating affects composition and oxidative stability of sesame (Sesamum indicum) oil. J. Food Sci. 59:613–16. doi:10.1111/jfds.1994.59.issue-3.
   Web of Science ®Google Scholar
• Yu, P. 2005. Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviors of protein: A novel approach. Br. J. Nutr. 94:655–65. doi:10.1079/BJN20051532.
   PubMed Web of Science ®Google Scholar
• Yu, T. Y., J. D. Morton, S. Clerens, and J. M. Dyer. 2017. Cooking-induced protein modifications in meat. Compr. Rev.Food Sci.Food Saf. 16:141–59. doi:10.1111/crf3.2017.16.issue-1.
   PubMed Web of Science ®Google Scholar