Use of High-Intensity Ultrasound to Improve Functional Properties of Batter Suspensions Prepared from PSE-like Chicken Breast Meat

Food and Bioprocess Technology

Volumn 7, Issue 12, 2014, Pages 3466-3477

  Li, Ke ^a   Kang, Zhuang Li ^a   Zhao, Ying Ying ^a   Xu, Xing Lian ^a   Zhou, Guang Hong ^a  

^a NANJING AGRICULTURAL UNIVERSITY   (China)

Author keywords

Chicken; Functional properties; PSE; Raman spectroscopy; Ultrasound

Indexed keywords

ANIMALS; MEATS; MICROSTRUCTURE; PARTICLE SIZE; PARTICLE SIZE ANALYSIS; PROTEINS; RAMAN SPECTROSCOPY; RHEOLOGY; SUSPENSIONS (FLUIDS);

CHICKEN; FUNCTIONAL PROPERTIES; HIGH INTENSITY ULTRASOUNDS; PROTEIN SECONDARY STRUCTURE; RHEOLOGICAL BEHAVIORS; RHEOLOGICAL PROPERTY; ULTRASOUND TREATMENTS; WATER HOLDING CAPACITY;

ULTRASONICS;

EID: 84919913851     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-014-1358-y     Document Type: Article

References (59)

1. Alix, A. J. P., Pedanou, G., & Berjot, M. (1988). Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band. Journal of Molecular Structure, 174, 159–164.
2. AOAC, (2000). Official methods of analysis of AOAC international (17th ed.), AOAC International, Gaithersburg, MD, USA.
3. Arzeni, C., Martínez, K., Zema, P., Arias, A., Pérez, O. E., & Pilosof, A. M. R. (2012a). Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108, 463–472.
4. Arzeni, C., Pérez, O. E., & Pilosof, A. M. R. (2012b). Functionality of egg white proteins as affected by high intensity ultrasound. Food Hydrocolloids, 29, 308–316.
5. Awad, T. S., Moharram, H. A., Shaltout, O. E., Asker, D., & Youssef, M. M. (2012). Applications of ultrasound in analysis, processing and quality control of food: a review. Food Research International, 48, 410–427.
6. Barbut, S. (1997). Microstructure of white and dark turkey meat batters as affected by pH. British Poultry Science, 38(2), 175–182.
7. Barbut, S. (2009). Pale, soft, and exudative poultry meat—reviewing ways to manage at the processing plant. Poultry Science, 88, 1506–1512.
8. Barbut, S., Sosnicki, A. A., Lonergan, S. M., Knapp, T., Ciobanu, D. C., Gatcliffe, L. J., Huff-Lonergan, E., & Wilson, E. W. (2008). Progress in reducing the pale, soft and exudative (PSE) problem in pork and poultry meat. Meat Science, 79, 46–63.
9. Bevilacqua, A., Sinigaglia, M., & Corbo, M. R. (2013). Ultrasound and antimicrobial compounds: a suitable way to control Fusarium oxysporum in juices. Food and Bioprocess Technology, 6(5), 1153–1163.
10. Cárcel, J. A., Benedito, J., Bon, J., & Mulet, A. (2007). High intensity ultrasound effects on meat brining. Meat Science, 76, 611–619.
11. Chandrapala, J., Zisu, B., Palmer, M., Kentish, S., & Ashokkumar, M. (2011). Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrasonics Sonochemistry, 18, 951–957.
12. Chandrapala, J., Oliver, C., Kentish, S., & Ashokkumar, M. (2012). Ultrasonics in food processing. Ultrasonics Sonochemistry, 19(5), 975–983.
13. Chang, H. J., Xu, X. L., Zhou, G. H., Li, C. B., & Huang, M. (2012). Effects of characteristics changes of collagen on meat physicochemical properties of beef semitendinosus muscle during ultrasonic processing. Food and Bioprocess Technology, 5, 285–297.
14. Droval, A. A., Benassi, V. T., Rossa, A., Prudencio, S. H., Paião, F. G., & Shimokomaki, M. (2012). Consumer attitudes and preferences regarding pale, soft, and exudative broiler breast meat. Journal of Applied Poultry Research, 21, 502–507.
15. Egelandsdal, B., Fretheim, K., & Samejima, K. (1986). Dynamic rheological measurements on heat-induced myosin gels: effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate. Journal of Science and Food Agriculture, 37, 915–926.
16. Ferris, J. J., Sandoval, A. J., Barreiro, J. A., Sánchez, J. J., & Müller, A. J. (2009). Gelation kinetics of an imitation-mortadella emulsion during heat treatment determined by oscillatory rheometry. Journal of Food Engineering, 95, 677–683.
17. Garcia, R. G., de Freitas, L. W., Schwingel, A. W., Farias, R. M., Caldara, F. R., Gabriel, A. M. A., Graciano, J. D., Komiyama, C. M., & Almeida Paz, I. C. L. (2010). Incidence and physical properties of PSE chicken meat in a commercial processing plant. Brazilian Journal of Poultry Science, 4, 233–237.
18. Gornall, A. G., Baradawill, C. J., & David, M. M. (1949). Determination of serum protein by means of the biuret reaction. Journal of Biological Chemistry, 177, 751–766.
19. Gülseren, I., Güzey, D., Bruce, B. D., & Weiss, J. (2007). Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrasonics Sonochemistry, 14, 173–183.
20. Han, M., Zhang, Y., Fei, Y., Xu, X., & Zhou, G. (2009). Effect of microbial trans-glutaminase on NMR relaxometry and microstructure of pork myofibrillar protein gel. European Food Research and Technology, 228(4), 665–670.
21. Herrero, A. M. (2008). Raman spectroscopy a promising technique for quality assessment of meat and fish: a review. Food Chemistry, 107, 1642–1651.
22. Honikel, K. O. (1998). Reference methods for the assessment of physical characteristics of meat. Meat Science, 49, 447--457.
23. Horžić, D., Jambrak, A. R., Belščak-Cvitanović, A., Komes, D., & Lelas, V. (2012). Comparison of conventional and ultrasound assisted extraction techniques of yellow tea and bioactive composition of obtained extracts. Food and Bioprocess Technology, 5(7), 2858–2870.
24. Hu, H., Fan, X., Zhou, Z., Xu, X. Y., Fan, G., Wang, L. F., Huang, X. J., Pan, S. Y., & Zhu, L. (2013a). Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pretreatments. Ultrasonics Sonochemistry, 20(1), 187–195.
25. Hu, H., Li-Chan, E. C. Y., Wan, L., Tian, M., & Pan, S. Y. (2013b). The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32, 303–311.
26. Hu, H., Wu, J. H., Li-Chan, E. C. Y., Zhu, L., Zhang, F., Xu, X. Y., Fan, G., Wang, L. F., Xingjian Huang, X. J., & Pan, S. Y. (2013c). Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids, 30, 647–655.
27. Jambrak, A. R., Mason, T. J., Lelas, V., Herceg, Z., & Herceg, I. L. (2008). Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering, 86, 281–287.
28. Jambrak, A. R., Herceg, Z., Šubarić, D., Babić, J., Brnčić, M., Brnčić, S. R., Bosiljkov, T., Čvek, D., Tripalo, B., & Gelo, J. (2010). Ultrasound effect on physical properties of corn starch. Carbohydrate Polymers, 79, 91–100.
29. Jambrak, A. R., Mason, T. J., Lelas, V., Paniwnyk, L., & Herceg, Z. (2014). Effect of ultrasound treatment on particle size and molecular weight of whey proteins. Journal of Food Engineering, 121, 15–23.
30. Jayasooriya, S. D., Bhandari, B. R., Torley, P., & D’Arcy, B. R. (2004). Effect of high power ultrasound waves on properties of meat: a review. International Journal of Food Properties, 7(2), 301–319.
31. Jayasooriya, S. D., Torley, P. J., D’Arcy, B. R., & Bhandari, B. R. (2007). Effect of high power ultrasound and ageing on the physical properties of bovine semitendinosus and longissimus muscles. Meat Science, 75, 628–639.
32. Jiang, J., & Xiong, Y. L. (2013). Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase. Meat Science, 93(3), 469–476.
33. Laemmli, V. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.
34. Lesiów, T., & Xiong, Y. L. (2001). Mechanism of rheological changes in poultry myofibrillar proteins during gelation. Avian & Poultry Biology Reviews, 12, 137–149.
35. Li, C., Huang, X., Peng, Q., Shan, Y., & Xue, F. (2014). Physicochemical properties of peanut protein isolate-glucomannan conjugates prepared by ultrasonic treatment. Ultrasonics Sonochemistry. doi:10.1016/j.ultsonch.2014.03.018.
36. Liu, R., Zhao, S. M., Xiong, S. B., Xie, B. J., & Liu, H. M. (2007). Studies on fish and pork paste gelation by dynamic rheology and circular dichroism. Journal of Food Science, 72(7), E399–E403.
37. Liu, R., Zhao, S. M., Xiong, S. B., Xie, B. J.,& Qin, L. H. (2008). Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science, 80, 632–639.
38. Liu, R., Zhao, S. M., Liu, Y. M., Yang, H., Xiong, S. B., Xie, B. J., & Qin, L. H. (2010). Effect of pH on the gel properties and secondary structure of fish myosin. Food Chemistry, 121, 196–202.
39. Madadlou, A., Emam-Djomeh, Z., Mousavi, M. E., Mohamadifar, M., & Ehsani, M. (2010). Acid-induced gelation behavior of sonicated casein solutions. Ultrasonics Sonochemistry, 17, 153–158.
40. McDonnell, C. K., Allen, P., Morin, C., & Lyng, J. G. (2014). The effect of ultrasonic salting on protein and water-protein interactions in meat. Food Chemistry, 147, 245–251.
41. Omana, D. A., Moayedi, V., Xu, Y., & Betti, M. (2010). Alkali-aided protein extraction from chicken dark meat: textural properties and color characteristics of recovered proteins. Poultry Science, 89, 1056–1064.
42. Petracci, M., Bianchi, M., Mudalala, S., & Cavani, C. (2013). Functional ingredients for poultry meat products. Trends in Food Science and Technology, 33, 27–39.
43. Pietrzak, M., Greaser, M. L., & Sosnicki, A. A. (1997). Effect of rapid rigor mortis processes on protein functionally in pectoralis major muscle of domestic turkeys. Journal of Animal Science, 75, 2106–2116.
44. Poulter, R. G., Ledward, D. A., Godber, S., Hall, G., & Rowlands, B. (1985). Heat stability of fish muscle proteins. Journal of Food Technology, 20, 203–217.
45. Rastogi, N. (2011). Opportunities and challenges in application of ultrasound in food processing. Critical Reviews in Food Science & Nutrition, 51, 705–722.
46. Shao, J. H., Zou, Y. F., Xu, X. L., Wu, J. Q., & Zhou, G. H. (2011). Evaluation of structural changes in raw and heated meat batters prepared with different lipids using Raman spectroscopy. Food Research International, 44, 2955–2961.
47. Somboonpanyakul, P., Barbut, S., Jantawat, P., & Chinprahast, N. (2007). Increasing the salt level resulted in an overall increase of cook yield, textural and sensory quality of poultry meat batter containing malva nut gum, salt and phosphate. LWT- Food Science and Technology, 40, 498–505.
48. Soria, A. C., & Villamiel, M. (2010). Effect of ultrasound on the technological properties and bioactivity of food: a review. Trends in Food Science and Technology, 21(7), 323–331.
49. Stadnik, J., & Dolatowski, Z. J. (2011). Influence of sonication on Warner-Bratzler shear force, colour and myoglobin of beef (M. semimembranosus). European Food Research Technology, 233, 553–559.
50. Sun, Y. J., Chen, J. H., Zhang, S. W., Li, H. J., Lu, J., Liu, L., Uluko, H., Su, Y. L., Cui, W. M., Ge, W. P., & Lv, J. P. (2014). Effect of power ultrasound pre-treatment on the physical and functional properties of reconstituted milk protein concentrate. Journal of Food Engineering, 124, 11–18.
51. Wang, H. L., Pato, M., Pietrasik, Z., & Shand, P. (2009). Biochemical and physicochemical properties of thermally treated natural actomyosin extracted from normal and PSE pork longissimus muscle. Food Chemistry, 113, 21–27.
52. Wilhelm, A. E., Maganhini, M. B., Hernandez-Blazquez, F. J., Ida, E. I., & Shimokomaki, M. (2010). Protease activity and the ultrastructure of broiler chicken PSE (pale, soft, exudative) meat. Food Chemistry, 119, 1201–1204.
53. Xiong, Y. L. (1994). Myofibrillar protein from different muscle fiber types: implications of biochemical and functional properties in meat processing. Critical Reviews in Food Science and Nutrition, 34(3), 293–320.
54. Xiong, Y. L. (1997). Structure-functionality relationships of muscle proteins. In S. Damodaran & A. Paraf (Eds.), Food protein and their application (pp. 341–392). New York: Marcel Dekker, Inc.
55. Zhang, L., & Barbut, S. (2005). Rheological characteristics of fresh and frozen PSE, normal and DFD chicken breast meat. British Poultry Science, 46, 687–693.
56. Zhou, F. B., Zhao, M. M., Zhao, H. F., Sun, W. Z., & Cui, C. (2014). Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals. Meat Science, 96(4), 1432–1439.
57. Zhu, X., Ruusunen, M., Gusella, M., Zhou, G., & Puolanne, E. (2011). High post-mortem temperature combined with rapid glycolysis induces phosphorylase denaturation and produces pale and exudative characteristics in broiler pectoralis major muscles. Meat Science, 89, 181–188.
58. Zhu, X. S., Xu, X. L., Min, H. H., & Zhou, G. H. (2012). Occurrence and characterization of pale, soft, exudative-like broiler muscle commercially produced in China. Journal of Integrative Agriculture, 11(8), 1384–1390.
59. Zisu, B., Bhaskaracharya, R., Kentish, S., & Ashokkumar, M. (2010). Ultrasonic processing of dairy systems in large scale reactors. Ultrasonics Sonochemistry, 17, 1075–1081.