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Quality parameters of chicken breast meat affected by carcass scalding conditions

Silva-Buzanello, Rosana Aparecida da;Schuch, Alexia Francielli;Gasparin, Andre Wilhan;Torquato, Alex Sanches;Scremin, Fernando Reinoldo;Canan, Cristiane;Soares, Adriana Lourenco

  • Received : 2018.09.11
  • Accepted : 2019.01.09
  • Published : 2019.08.01

Abstract

Objective: The influence of broiler carcass scalding conditions on chicken breast meat quality parameters was investigated. Methods: Two hundred and seventy Cobb broiler chickens from 42 to 48 days old were slaughtered according to the standard industry practice and scalded in five temperature/time combinations-$T_1$, $54^{\circ}C/210s$; $T_2$, $55^{\circ}C/180s$; $T_3$, $56^{\circ}C/150s$; $T_4$, $57^{\circ}C/120s$; $T_5$, $58^{\circ}C/90s$. Results: Scalding temperature increase resulted in higher values of external and ventral lightness and in protein functionality reduction-determined by emulsification capacity and protein denaturation-in chicken breast fillets 24 h post-mortem. Protein secondary structures had conformational changes, with a decrease of the ${\alpha}$-helix and an increase of the ${\beta}$-sheet and ${\beta}$-turn proportions, mainly in $T_1$ and $T_5$ samples, determined by Fourier-transform infrared spectroscopy in an attenuated reflectance mode analysis. The chemical composition, pH, water holding capacity and Warner-Bratzler shear force did not differ among the treatments. In the fatty acid profile, the 18:1n-9 was lower in $T_5$, which suggested that the high scalding-temperature could have caused the lipid oxidation. The values of the polyunsaturated fatty acids (PUFA), such as 22:2, 20:4n-6, and 22:6n-3, were highest in the $T_5$, thus being related to the phospholipid cellular membrane collapse in this experimental condition and subsequent release of these PUFA. Conclusion: Intermediate scalding-parameters avoided the negative changes in the chicken meat quality.

Keywords

Emulsification Capacity;Fatty Acid Profile;Protein Denaturation;Protein Secondary Structure

References

  1. Cason JA, Buhr RJ, Hinton A. Unheated water in the first tank of a three-tank broiler scalder. Poult Sci 2001;80:1643-6. https://doi.org/10.1093/ps/80.11.1643 https://doi.org/10.1093/ps/80.11.1643
  2. Sams AR, McKee SR. First processing: slaughter through chilling. In: Owens CM, Alvarado CZ, Sams AR, editors. Poult meat process. 2nd ed. Boca Raton, FL, USA: CRC Press; 2010. p. 25-50.
  3. Buhr RJ, Walker JM, Bourassa DV, Caudill AB, Kiepper BH, Zhuang H. Impact of broiler processing scalding and chilling profiles on carcass and breast meat yield. Poult Sci 2014;93:1534-41. https://doi.org/10.3382/ps.2013-03535 https://doi.org/10.3382/ps.2013-03535
  4. McKee SR, Townsend JC, Bilgili SF. Use of a scald additive to reduce levels of Salmonella Typhimurium during poultry processing. Poult Sci 2008;87:1672-7. https://doi.org/10.3382/ps.2008-00061 https://doi.org/10.3382/ps.2008-00061
  5. Jeong JY, Janardhanan KK, Booren AM, Karcher DM, Kang I. Moisture content, processing yield, and surface color of broiler carcasses chilled by water, air, or evaporative air. Poult Sci 2011;90:687-93. https://doi.org/10.3382/ps.2010-00980 https://doi.org/10.3382/ps.2010-00980
  6. Bowker BC, Zhuang H, Buhr RJ. Impact of carcass scalding and chilling on muscle proteins and meat quality of broiler breast fillets. LWT - Food Sci Technol 2014;59:156-62. https://doi.org/10.1016/j.lwt.2014.05.008 https://doi.org/10.1016/j.lwt.2014.05.008
  7. Zhuang H, Bowker BC, Jeff Buhr R, Bourassa DV, Kiepper BH. Effects of broiler carcass scalding and chilling methods on quality of early-deboned breast fillets. Poult Sci 2013;92:1393-9. https://doi.org/10.3382/ps.2012-02814 https://doi.org/10.3382/ps.2012-02814
  8. Tornberg E. Effects of heat on meat proteins - Implications on structure and quality of meat products. Meat Sci 2005;70:493-508. https://doi.org/10.1016/j.meatsci.2004.11.021 https://doi.org/10.1016/j.meatsci.2004.11.021
  9. Olivo R, Soares AL, Ida EI. Dietary vitamin E inhibits poultry PSE and improves meat function properties. J Food Biochem 2001;25:271-83. https://doi.org/10.1111/j.1745-4514.2001.tb00740.x https://doi.org/10.1111/j.1745-4514.2001.tb00740.x
  10. Hamm R. Biochemistry of meat hydration. Adv Food Res 1960;10:355-463. https://doi.org/10.1016/S0065-2628(08)60141-X
  11. Olivo R, Shimokomaki M. Carnes: no caminho da pesquisa. 2nd ed. Cocal do Sul, Brazil: IMPRINT; 2002.
  12. Qiao M, Fletcher DL, Smith DP, Northcutt JK. The effect of broiler breast meat color on pH, moisture, water-holding capacity, and emulsification capacity. Poult Sci 2001;80:676-80. https://doi.org/10.1093/ps/80.5.676 https://doi.org/10.1093/ps/80.5.676
  13. Swatland HJ. Optical properties of meat. On-line evaluation meat. Lancaster, PA, USA: CRC Press; 1995. p. 126-9.
  14. Bligh EG, Dyer WJ. A rapid method of total lipid extraction and purification. Can J Biochem Physiol 1959;37:911-7. https://doi.org/10.1139/y59-099 https://doi.org/10.1139/y59-099
  15. International Organization for Standardization. ISO 5509: animal and vegetable fats and oils: preparation of methyl esters of fatty acids. London, UK: International Organization for Standardization; 1978.
  16. Kong J, Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin (Shanghai). 2007;39:549-59. https://doi.org/10.1111/j.1745-7270.2007.00320.x https://doi.org/10.1111/j.1745-7270.2007.00320.x
  17. AOAC. Fat, moisture and protein in meat and meat products. FOSS foodscan near-infrared (NIR) spectrophotometer with FOSS artificial neural network (ANN) calibration model and associated. J AOAC Int 2007;90:1073-83.
  18. AOAC. Official methods of analysis of the Association of Official Analytical Chemists. 18th ed. Arlington, VA, USA: AOAC International; 2005.
  19. Jiang H, Yoon SC, Zhuang H, Wang W. Predicting color traits of intact broiler breast fillets using visible and near-infrared spectroscopy. Food Anal Methods 2017;10:3443-51. https://doi.org/10.1007/s12161-017-0907-1 https://doi.org/10.1007/s12161-017-0907-1
  20. Kato T, Barbosa CF, Ida EI, Soares AL, Shimokomaki M, Pedrao MR. Broiler chicken PSE (pale, soft, exudative) meat and water release during chicken carcass thawing and Brazilian legislation. Braz Arch Biol Technol 2013;56:996-1001. http://dx.doi.org/10.1590/S1516-89132013000600015 https://doi.org/10.1590/S1516-89132013000600015
  21. Silva-Buzanello RA da, Schuch AF, Nunes Nogues DR, et al. Physicochemical and biochemical parameters of chicken breast meat influenced by stunning methods. Poult Sci 2018;97:3786-92. https://doi.org/10.3382/ps/pey281 https://doi.org/10.3382/ps/pey281
  22. Wilhelm AE, Maganhini MB, Hernandez-Blazquez FJ, Ida EI, Shimokomaki M. Protease activity and the ultrastructure of broiler chicken PSE (pale, soft, exudative) meat. Food Chem 2010;119:1201-4. https://doi.org/10.1016/j.foodchem.2009.08.034 https://doi.org/10.1016/j.foodchem.2009.08.034
  23. Strasburg G, Xiong YL, Chiang W. Physiology and chemistry of edible muscle tissues. Quimica Aliment Fennema. 4th ed. Porto Alegre, RS, Brazil: Artmed; 2010. pp. 719-54.
  24. Brazil. Instrucao Normativa no 32 de 03 de dezembro de 2010. Parameters for evaluation of the total water content in cold and frozen chicken cuts. Brasilia, Brazil: Ministerio da Agricultura, Pecuaria e Abastecimento; 2010. p. 2010.
  25. Liu R, Zhao SM, Xiong SB, Xie BJ, Qin LH. Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Sci 2008;80:632-9. https://doi.org/10.1016/j.meatsci.2008.02.014 https://doi.org/10.1016/j.meatsci.2008.02.014
  26. Damodaran S. Amino acids, peptides and proteins. In: Damodaran S, Parkin KL, Fennema OR, editors. Quimica aliment fennema. 4th ed. Porto Alegre, RS, Brazil: Artmed; 2010. p. 900.
  27. Xu XL, Han MY, Fei Y, Zhou GH. Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic. Meat Sci 2011;87:159-64. https://doi.org/10.1016/j.meatsci.2010.10.001 https://doi.org/10.1016/j.meatsci.2010.10.001
  28. Murakami M, Kudo I. Phospholipase A2. J Biochem 2002;131:285-92. https://doi.org/10.1093/oxfordjournals.jbchem.a003101 https://doi.org/10.1093/oxfordjournals.jbchem.a003101
  29. Soares AL, Ida EI, Miyamoto S, Hernandez-Blazque FJ, Olivo R, Pinheiro JW, et al. Phospholipase A2 activity in poultry PSE, pale, soft, exudative, meat. J Food Biochem 2003;27:309-20. https://doi.org/10.1111/j.1745-4514.2003.tb00285.x https://doi.org/10.1111/j.1745-4514.2003.tb00285.x
  30. Lambert IH, Nielsen JH, Andersen HJ, ortenblad N. Cellular model for induction of drip loss in meat. J Agric Food Chem 2001;49:4876-83. https://doi.org/10.1021/jf010121y https://doi.org/10.1021/jf010121y
  31. Morgado MAP, Cabral JMS, Prazeres DMF. Hydrolysis of lecithin by phospholipase A2 in mixed reversed micelles of lecithin and sodium dioctyl sulphosuccinate. J Chem Technol Biotechnol 1995;63:181-9. https://doi.org/10.1002/jctb.280630214 https://doi.org/10.1002/jctb.280630214
  32. Belhadj Slimen I, Najar T, Ghram A, Abdrrabba M. Heat stress effects on livestock: molecular, cellular and metabolic aspects, a review. J Anim Physiol Anim Nutr (Berl) 2016;100:401-12. https://doi.org/10.1111/jpn.12379 https://doi.org/10.1111/jpn.12379