Comparison Between Conventional Convective Heating and Microwave Heating: An FTIR Spectroscopy Study of the Effects of Microwave Oven Cooking of Bovine Breast Meat

Emanuele Calabrò, Salvatore Magazù

Department of Physics, University of Messina, Messina, Italy..

DOI: 10.4236/jemaa.2012.411060                

Abstract

The effects of microwave energy and conventional convective heating on bovine meat were studied in the mid-infrared region by FTIR spectroscopy, to highlight the differences between the two cooking methods. Samples of 100 g of bovine breast meat were cooked using three treatments: heating in a conventional electric oven at the temperature of 165°C for 16 min, heating in a microwave oven at 800 W for 95 sec, and heating in the same microwave oven at 650 W for 160 sec. Significant decreases in intensity of vibration bands of CH2 methylene group at 1921 and 1853 cm-1 and of the carbonyl band at 1742 cm-1 were observed after microwave heating with respect to heating in a conventional oven, showing that Maillard reaction occurs partially using microwave oven. Spectral analysis in the amide I region after microwave cooking at 800 W for 95 sec showed that an increase in intensity occurred in the region from 1665 to 1690 cm-1 which can be attributed to β-turns, characteristic of disorder processes in the protein. Further analysis after microwave cooking at 650 W for 160 sec evidenced major increase in intensity of β-turns content and the appearance of significant increases of β-sheet component at 1635 cm-1 and 1695 cm-1 that can be attributed to aggregated β-sheets structures.

Keywords

Convective heating; Microwave oven; FTIR spectroscopy; Amide I region; Bovine breast meat

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1]	E. Tornberg, “Effects of Heat on Meat Proteins—Implications on Structure and Quality of Meat Products,” Meat Science, Vol. 70, No. 3, 2005, pp. 493-508. doi:10.1016/j.meatsci.2004.11.021
[2]	M. Kumar and B. D. Sharma, “The Storage Stability and Textural, Physico-Chemical and Sensory Quality of LowFat Ground Pork Patties with Car-rageenan as Fat Replacer,” International Journal of Food Science & Technology, Vol. 39, No. 1, 2004, pp. 31-42. doi:10.1111/j.1365-2621.2004.00743.x
[3]	S. H. Ko, S.-H. Yoo, S. Y. Lee, S. H. Cho, K.-H. Kim and R. Hwang, “Effect of Long Low Temperature-Short High Temperature Cooking Cycle on Physicochemical Properties of Beef,” Food Science and Technology Research, Vol. 17, No. 1, 2011, pp. 11-16.
[4]	T. H. Powell, M. E. Dikeman and M. C. Hunt, “Tenderness and Collagen Composition of Beef Semitendinosus Roasts Cooked by Conventional Convective Cooking and Modeled, Multi-Stage, Convective Cooking,” Meat Science, Vol. 55, No. 4, 2000, pp. 421-425. doi:10.1016/S0309-1740(99)00171-0
[5]	L. E. Jeremiah and L. L. Gibson, “Cooking Influences on the Palatability of Roasts from the Beef Hip,” Food Research International, Vol. 36, No. 1, 2003, pp. 1-9. doi:10.1016/S0963-9969(02)00093-5
[6]	D. M. P. Mingos and D. R. Baghurst, “Application of Microwave Dielectric Heating Effects to Synthetic Problems in Chemistry,” In: H. M. Kingston and S. J. Haswell, Eds., Microwave-Enhanced Che-mistry. Fundamentals, Sample Preparation and Applications, ACS Publications, Washington, 1997, pp. 3-53.
[7]	T. Ohlsson, “Domestic Use of Microwave Ovens,” In: R. Macrae, R. K. Robinson and M. J. Sadler, Eds., Encyclopaedia of food science food technology and nutrition, Academic Press, London, 1993, pp. 1232-1237.
[8]	C. R. Buffler, “Microwave Cooking and Processing: Engineering Fundamentals for the Food Scientist,” Van Nostrand Reinhold, New York, 1993.
[9]	L. Fulton and C. Davis, “Roasting and Braising Beef Roasts in Microwave Ovens,” Journal of the American Dietetic Associa-tion, Vol. 83, No. 5, 1983, p. 560.
[10]	V. D. Pawar, F. A. Khan and B. S. Agarkar, “Effect of Fat/Whey Protein Concen-trate Levels and Cooking Methods on Textural Characteristics of Chevon Patties,” Journal of Food Science and Technology, Vol. 39, No. 4, 2002, pp. 429-431.
[11]	T. Albi, A. Lanzon, A. Guinda, M. C. Pérez-Camino and M. Leon, “Microwave and Conventional Heating Effects on Some Physical and Chemical Parameters of Edible Fats,” Journal of Agricultural and Food Chemistry, Vol. 45, No. 8, 1997, pp. 3000-3003. doi:10.1021/jf970168c
[12]	H. Yoshida, N. Hirooka and G. Kajimoto, “Microwave Heating Effects on Relative Stabilities of Tocopherols in Oils,” Journal of Food Science, Vol. 56, No. 4, 1991, pp. 1042-1046. doi:10.1111/j.1365-2621.1991.tb14637.x
[13]	H. Yoshida and G. Kajimoto, “Microwave Heating Affects Composition and Oxidative Stability of Sesame (Sesamum indicum) oil,” Journal of Food Science, Vol. 59, No. 3, 1994, pp. 613-616. doi:10.1111/j.1365-2621.1994.tb05575.x
[14]	S. M. Herzallah, “Influence of Microwaving and Conventional Heating of Milk on Cholesterol Contents and Cholesterol Oxides Formation,” Pakistan Journal of Nutrition, Vol. 4, No. 2, 2005, pp. 85-88. doi:10.3923/pjn.2005.85.88
[15]	P. Yu, S. Tamminga, A. R. Egan and D. A. Christensen, “Probing Equivocal Effects of Heat Processing of Legume Seeds on Performance of Ruminants—A Review,” Asian-Australasian Journal of Animal Sciences, Vol. 17, No. 6, 2004, pp. 869-876.
[16]	F. R. Van de Voort, “Fourier Transform Infrared Spectroscopy Applied to Food Analysis,” Food Research International, Vol. 25, No. 5, 1992, pp. 397-403. doi:10.1016/0963-9969(92)90115-L
[17]	K. F. Ng-Kwai-Hang, J. E. Moxley and F. R. van de Voort, “Factors Affecting Dif-ferences in Milk Fat Test Obtained by Babcock, Rose-Gottlieb and Infrared Methods and in Protein Test From Infrared Milk Analysis,” Journal of Dairy Science, Vol. 71, No. 2, 1988, pp. 290298. doi:10.3168/jds.S0022-0302(88)79557-0
[18]	J. M. Olinger and P. R. Griffiths, “Effects of Sample Dilution and Particle Size/Morphology on Diffuse Reflection Spectra of Carbohydrate Systems in the Nearand Mid-Infrared. Part 1: Single Analytes,” Applied Spectroscopy, Vol. 47, No. 6, 1993, pp. 687-694. doi:10.1366/0003702934066965
[19]	W. K. Surewicz and H. H. Mantsch, “New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra,” Biochim et Biophys Acta, Vol. 952, No. 2, 1988, pp. 115-130. doi:10.1016/0167-4838(88)90107-0
[20]	B. Stuart, “Infrared Spectroscopy: Fundamentals and Applications,” John Wiley & Sons, Hoboken, 2004.
[21]	P. Dumas and L. Miller, “The Use of Synchrotroninfraredmicrospectroscopy in Biological and Biomedical Investigations,” Vibrational Spectroscopy, Vol. 32, No. 1, 2003, pp. 3-21. doi:10.1016/S0924-2031(03)00043-2
[22]	L. C. Maillard, “Action des acides aminés sur les sucres; formation des méla-noidines par voie methodique,” Comptes Rendus de l'Académie des Sciences, Vol. 154, 1912, pp. 66-68.
[23]	J. E. Hodge, “Dhydrated Foods. Chemistry of Browning Reaction in Model Systems,” Journal of Agricultural and Food Chemistry, Vol. 1, No. 15, 1953, pp. 928-943. doi:10.1021/jf60015a004
[24]	M. Namiki, “Chemistry of Maillard Reactions: Recent Studies on the Browning Reaction Mechanism and the Development of Antioxidants and Muta-gens,” Advances in Food Research, Vol. 32, 1988, pp. 115-184. doi:10.1016/S0065-2628(08)60287-6
[25]	E. Calabrò and S. Magazù, “Inspections of Mobile Phone Microwaves Effects on Proteins Secondary Structure by means of Fourier Transform Infrared Spectroscopy,” Journal of Electromagnetic Analysis & Applications, Vol. 2, No. 11, 2010, pp. 607-617. doi:10.4236/jemaa.2010.211080
[26]	E. Calabrò, S. Condello, M. Currò, N. Ferlazzo, D. Caccamo, S. Magazù and R. Ientile, “Modulation of HSP Response in SH-SY5Y Cells Following Exposure to Microwaves of a Mobile Phone,” World Journal of Biological Chemistry, Vol. 3, No. 2, 2012, pp. 34-40. doi:10.4331/wjbc.v3.i2.34
[27]	E. Calabrò and S. Magazù, “Electromagnetic Fields Effects on the Secondary Structure of Lysozyme and Bioprotective Effectiveness of Trehalose,” Ad-vances in Physical Chemistry, Vol. 2012, 2012, Article ID 970369, 6 pages. doi:10.1155/2012/970369
[28]	E. Calabrò, S. Magazù and S. Campo, “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,” Research Journal of Chemistry and Environment, 2012, accepted and in press.
[29]	M. Jackson and H. H. Mantsch, “The Use and Mi-suse of FTIR Spectroscopy in the Determination of Protein Structure,” Critical Reviews in Biochemistry and Molecular Biology, Vol. 30, No. 2, 1995, pp. 95-120. doi:10.3109/10409239509085140
[30]	J. Kong and S. Yu, “Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures,” Acta Biochimica et Biophysica Sinica, Vol. 39, No. 8, 2007, pp. 549-559. doi:10.1111/j.1745-7270.2007.00320.x
[31]	H. Fabian and W. M?ntele, “Infrared Spectroscopy of Proteins,” In: J. M. Chal-mers and P. R. Griffiths, Eds., Handbook of Vibrational Spec-troscopy, John Wiley & Sons Ltd., Chichester, 2002, pp. 3399-3425.