INVESTIGATING THE EFFECTS OF SALT, PHOSPHATE AND PH ON FUNCTIONAL PROPERTIES OF BEEF MYOFIBRILLAR PROTEINS

Öz

This study aimed to investigate the effect of salt and phosphate on the functional properties of myofibrillar proteins (MPs) at pH 2, 4, 6, 8, and 10. The highest emulsion activity index (EAI) value (8.51 m²/g protein) was obtained with the use of NaCl, and phosphate at pH 10. The highest emulsion stability index (ESI) result was determined (230.8 minutes) with the use of salt at pH 8. The addition of salt and phosphate significantly (p<0.05) improved the emulsifying properties of proteins. Considering the water absorption capacity (WAC), the highest value was obtained as 1.9 mL water/g protein at pH 6 and pH 8. The highest fat absorption capacity (FAC) value of 8.3 mL fat/g protein was found with the addition of phosphate at pH 6. The highest foam capacity (FC) and foam stability (FS) were obtained at pH 10 and 4, respectively.

Anahtar Kelimeler

• myofibrillar proteins
• functional proteins
• emulsion
• foam

DANA ETİ MİYOFİBRİLER PROTEİNLERİNİN FONKSİYONEL ÖZELLİKLERİ ÜZERİNE TUZ, FOSFAT ve PH’NIN ETKİLERİNİN ARAŞTIRILMASI

Öz

Bu çalışmada, tuzun ve fosfatın miyofibriler proteinlerin fonksiyonel özellikleri üzerindeki etkisinin pH 2, 4, 6, 8, 10 değerlerinde araştırılması amaçlanmıştır. Emülsiyon aktivite indeksi (EAI), emülsiyon stabilite indeksi (ESI), köpük kapasitesi (FC), köpük stabilitesi (FS), su absorpsiyon kapasitesi (WAC) ve yağ tutma kapasitesi (FAC) incelenmiştir. pH 10'da tuz ve fosfat kullanımıyla, en yüksek EAI değeri (8,51 m²/g protein) elde edilmiştir. pH 8'de, tuz kullanımıyla en yüksek ESI sonucu (230,8 dakika) belirlenmiş; tuz ve fosfat ilavesinin, proteinlerin emülsifiye edici özelliklerini önemli ölçüde iyileştirdiği (p<0.05) tespit edilmiştir. Fosfat ilavesiyle, pH 6 ve pH 8'de en yüksek WAC değeri (1,9 mL su/g protein) elde edilmiştir. En yüksek FAC değeri (8.3 mL yağ/g protein) pH 6'da fosfat ilavesiyle elde edilmiştir. Köpürme özelliklerine bakıldığında, en yüksek FC değeri pH 10'da (%90) elde edilmiştir. Fosfat ve tuz kombinasyonunda, pH 4'te, en yüksek FS sonucu %100 olarak belirlenmiştir.

Anahtar Kelimeler

• miyofibriler proteinler
• fonksiyonel özellikler
• emülsiyon
• köpük

Kaynakça

1. Amiri, A., Sharifian, P., Soltanizadeh, N. (2018). Application of ultrasound treatment for improving the physicochemical, functional and rheological properties of myofibrillar proteins. Int J Bio Macromol, 111: 139–147.
2. Ashie, I.N.A., Sorensen, T.L., Nielsen, P.M. (2002). Effects of papain and a microbial enzyme on meat proteins and beef tenderness. J Food Sci, 67, 6.
3. Barbut, S. (1995). Importance of fat emusification and protein matrix characteristics in meat batter stability. J Muscle Foods, 6:161.
4. Barbut, S., Mittal, G.S. (1988). Rheological and gelation properties of meat batters prepared with three chloride salts. J Food Sci, 53:1296.
5. Bendall, J.R. (1954). The swelling effect of polyphosphates on lean meat. J Sci Food Agric 5:468.
6. Bertram, H. C., Kristensen, M., Andersen, H.J. (2004). Functionality of myofibrillar proteins as affected by pH, ionic strength and heat treatment – a low-field NMR study. Meat Sci 68: 249–256.
7. Billeter, R., Heizmann, C. W., Reist, U., Howald, H., Jenny, E. (1982). Two-dimensional peptide analyses of myosin heavy chains and actin from single-typed human skeletal muscle fibers. FEBS Lett, 139, 45.
8. Cabra, V., Arreguin, R., Farres, A. (2008). Emulsifying properties of proteins. Bol Soc Quím Méx, 2(2): 80-89.

9. Chan JT, Omana DA, Betti M. (2011). Functional and rheological properties of proteins in frozen turkey breast meat with different ultimate pH. Poult Sci 90(5): 1112-23. doi: 10.3382/ps.2010-01185.
10. Chang, H.J., Xu, X.L., Zhou, G.H., Li, C.B., Huang, M. (2012). Effects of characteristics changes of collagen onmeat physicochemical properties of beef semitendinosus muscle during ultrasonic processing, J Food Bioproc Technol 5: 285–297.
11. Chen, X., Li, Y., Zhou, R., Liu, D., Xu, X. (2017). Water-soluble myofibrillar proteins prepared by high-pressure homogenisation: a comparison study on the composition and functionality. Int J Food Sci Tech
12. Cheng, Q., Sun, D.W. (2008). Factors affecting the water holding capacity of red meat products: a review of recent research advances. Crit Rev Food Sci 48: 137–159.
13. Cheng, J., Zhu, M., Liu, X. (2020). Insight into the conformational and functional properties of myofibrillar protein modified by mulberry polyphenols. Food Chem, 308: 125592.
14. Choi, Y.M., Jung, K.C., Jo, H.M., Nam, K.W., Choe, J.H., Rhee, M.S., Kim, B.C. (2014). Combined effects of potassium lactate and calcium ascorbate as sodium chloride substitutes on the physicochemical and sensory characteristics of low-sodium frankfurter sausage. Meat Sci, 96: 21-25.
15. Clarke, F. M., Lovell, S. J., Masters, C. J., Winzor, D. J. (1976). Beef muscle troponin: Evidence for multiple forms of troponin-T, Biochim. Biophys Acta, 427: 617.
16. Colmenero, F.J., Borderias, A.J. (1983). A study of the effects of frozen storage on certain functional properties of meat and fish protein. Int J Food Sci Technol 18: 731-737. doi:10.1111/j.1365-2621.1983.tb00311.x
17. Damodaran, S. (1996). Amino acids, peptides, and proteins. In: Food Chemistry, Fennema, R. O. (Ed.), Marcel Dekker Inc, New York, USA. pp. 321–430.
18. Dhoot, G. K., Freason, N., Perry, S. V. (1979). Polymorphic forms of troponin T and troponin C and their localization in striated muscle cell types. Exp Cell Res 122: 339.
19. Dutson, T. R., Pearson, A. M., Merkel, R. A. (1974). Ultrastructural postmortem changes in normal and low-quality porcine muscle fibers. J Food Sci 39: 32.
20. Elizalde, B.E., Kanterewicz, R.J., Pilosof, A.M.R., Bartholomai G.B. (1988). Physicochemical properties of food proteins related to their ability to stabilize oil-in-water emulsions. J Food Sci 53(3): 845.
21. FAO (2006). World agriculture: Towards 2030/2050. Interim Report.Rome: Food and Agriculture Organisation.
22. Fernández-Martín F, Cofrades S, Carballo J, Jiménez-Colmenero F. (2002). Salt and phosphate effects on the gelling process of pressure/heat treated pork batters. Meat Sci 61(1): 15-23. doi: 10.1016/s0309-1740(01)00157-7.
23. Fligner, L., Mangino, E. (1991). Relationship of Composition to Protein Functionality. ACS Symposium Series; American Chemical Society: Washington, DC. Journal Article Number 43-90.
24. Forrest, J.C., Aberle, E.D., Hedrick, H.B., Merkel, R.A. (2001). Principle of Meat Science, 4th edition Kendall Hunt Pub Co, UK.
25. Fukazawa, T., Hashimoto, Y., Yasui, T. (1961). Effect of some proteins on the binding quality of an experimental sausage. J Food Sci 26:541.
26. Galluzzo, S.J., Regenstein, J.M. (1978). Role of chicken breast muscle proteins in meat emulsion formation: myosin, actin and synthetic actomyosin. J Food Sci 43: 1761.
27. Gauthier, G. F., Lowey, S. (1977). Polymorphism of myosin among skeletal muscle fiber types. J Cell Biol 74, 760, 1977.
28. Greaser, M. L., Gergely, J. (1971). Reconstitution of troponin activity from three protein components. J Biol Chem 246: 4226.
29. Hamm. (1986). Functional properties of the myofibrillar system and their measurements. In: Bechtel P. J., editor. Muscle as food. Academic Press, Inc; New York: pp. 135–199.
30. Hong, G.P., Chun, J.Y., Jo, Y.J., Choi, M.J. (2014). Effects of pH-shift processing and microbial transglutaminase on the gel and emulsion characteristics of porcine myofibrillar system. Korean J Food Sci Technol 34(2): 207-213.
31. Huff‐Lonergan, E., Lonergan, S. M., (2005). Mechanisms of water‐holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Sci 71: 194–204.
32. Ionescu, A., Aprodu, I., Daraba, A., Porneala, L. (2008). The effects of transglutaminase on the functional properties of the myofibrillar protein concentrate obtained from beef heart. Meat Sci 79: 278–284.
33. 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, Int J Food Prop 7 (2): 301–319.
34. Jones, K.W. (1984). Protein-lipid interaction in processed meats. Proceedings of 37th Annual Reciprocal Meat Conference, Lubbock, TX, p. 52.
35. Karthikeyan, M., Dileep, A.O., Shamasundar, B.A. (2005). Effect of water washing on the functional and rheological properties of proteins from threadfin bream (Nemipterus japonicus) meat. Int J Food Sci Technol 41: 1002–1010.
36. Khalili, A. D., Zarkadas, C. G. (1988). Determination of myofibrillar and connective tissue protein contents of young and adult avian (Gallus domesticus) skeletal muscles and the NT-methylhistidine content of avian actin. Poult Sci 67: 1593.
37. Kijowski, J., Niewiarowicz, A. (1978). Emulsifying properties of proteins and meat from broiler breast muscles as affected by their initial pH values. J Food Technol 13: 451-459.
38. Kim, T.K., Ku, S.K., Sung, J.M., Kim, Y.B., Kim, H.W., Choi, Y.S. (2018). Effects of marination and superheated steam process on quality characteristics of samgyetang. Korean J Food Cook Sci, 34: 155-162.
39. Kinsella, J. E., L. G. Phillips. (1989). Structure: functional relationship in food proteins, film and foaming behavior. Chapter 4, in J. E. Kinsella and W. G. Soucie, eds. Food proteins. American Oil Chemists' Society, Champaign, IL. pp. 52–77.
40. Kondaiah, N. et al., (1985). Effect of salt and phosphate on the quality of buffalo and goat meats. Meat Sci 15: 183-192.
41. Kudre, T.G., Bejjanki, S.K., Kanwate, B.W. Sakhare, P.Z. (2018). Comparative study on physicochemical and functional properties of egg powders from Japanese quail and white Leghorn chicken. Int J Food Prop 21: 956-971. doi: 10.1080/10942912.2018.1466320.
42. Laemmli, U. (1970). Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227: 680–685, https://doi.org/10.1038/227680a0.
43. Li‐Chan, E., Nakai, S., Wood, D.F. (1985). Relationship Between Functional (Fat Binding, Emulsifying) and Physicochemical Properties of Muscle Proteins. Effects of Heating, Freezing, pH and Species. J Food Sci 50: 1034-1040. https://doi.org/10.1111/j.1365-2621.1985.tb13006.x
44. Lili, L., Huan, W., Guangyue, R., Xu, D., Dan, L., Guangjun, Y. (2015). Effects of freeze-drying and spray drying processes on functional properties of phosphorylation of egg white protein. Int J Agric Biol Eng 8: 116-123.
45. Lin, T.M., Park, J.W. (1996). Extraction of proteins from pacific whiting mince at various washing conditions. J Food Sci 61(2): 432.
46. Malva, A., Albenzio, M., Santillo, A., Russo, D., Figliola, L., Caroprese, M., Marino, R. (2018). Methods for extraction of muscle proteins from meat and fish using denaturing and nondenaturing solutions. J Food Quality doi: 10.1155/2018/8478471.
47. Mathew, S., Shamasundar, B. A. (2002). Effect of ice storage on the functional properties of proteins from shark (Scoliodon laticaudus) meat. Nahrung/Food 46(4): 220–226.
48. Mohan, M., Ramachandran, D., Sankar, T.V. (2006). Functional properties of Rohu (Labeo rohita) proteins during iced storage. Food Res Int, 39: 847-854.
49. Nahar, Zakaria, Hashim, Bari, (2017). Effect of pH and salt concentration on protein solubility of slaughtered and non-slaughtered broiler chicken meat. Sains Malaysiana 46(5): 719–724.
50. Offer, G., Trinick, J. (1983). On the mechanism of water holding in meat: the swelling and shrinking of myofibrils. Meat Sci 8:245.
51. Omana, D. A., Xu, Y., Moayedi, V., Betti, M. (2010). Alkali-aided protein extraction from chicken dark meat: Chemical and functional properties of recovered proteins. Process Biochem 45(3): 375–381.
52. Parsons, N., Knight, P. (1990). Origin of variable extraction of myosin from myofibrils treated with salt and pyrophosphate. J Sci Food Agric 51:71.
53. Pearce, K.L., Rosenvold, K., Andersen, H.J., Hopkins, D.L., (2011). Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes: a review. Meat Sci 89: 111-124.
54. Pereira, P.M.C.C., Vicente, A.F.R.B. (2013). Meat nutritional composition and nutritive role in the human diet. Meat Sci, 93 (3): 586-592.
55. Pette, D., Staron, R. S. (1990). Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev Physiol Biochem Pharmacol 116, 2.
56. Puolanne E., Ruusunen M., Vainionpää J. (2001). Combined effects of NaCl and raw meat pH on water-holding in cooked sausage with and without added phosphate. Meat Sci, 58: 1-7.
57. Ramachandran, D., Mohan, M., Sankar, T.V., Anandan R. (2009). Physico-chemical and functional properties of myofibrillar proteins of fishes from different habitats. Fishery Technol 46(2):151 – 158.
58. Ramírez-Suárez, J.C., Xiong, Y.L. (2003). Effect of transglutaminase induced crosslinking on gelatin of myofibrillar/soy protein mixtures, Meat Sci 65: 899–907.
59. Richardson, R. I. and Jones, J. M. (1987). The effects of salt concentration and pH upon water binding, water holding and protein extractability of turkey meat. Int J Food Sci Technol 22: 683–692.
60. Robbins, J., Freyer, G. A., Chisholm, D., Gilliam, T. C. (1982). Isolation of multiple genomic sequences for chicken myosin heavy chain protein. J Biol Chem 257: 549.
61. Robbins, J., Horan, T., Gulick, J., Kropp, K. (1986). The chicken myosin heavy chain family. J Biol Chem 261: 6606.
62. Robe, G.H., Xiong, Y.L. (1993). Dynamic rheological studies on salt-soluble proteins from different porcine muscles. Food Hydrocolloids 7: 137.
63. Rocha-Estrada, J.G., Córdova-Murueta J.H., García-Carreno F.L. (2010). Functional properties of protein from frozen mantle and fin of jumbo squid dosidicus gigas in function of pH and ionic strength. Food Sci Technol Int 16: 451.
64. Romero, A., V. Beaumal, E. David-Briand, F. Cordobés, M. Anton, A. Guerrero. (2011). Interfacial and emulsifying behavior of crayfish protein isolate LWT – Food Sci Technol 44: 1603-1610.
65. Rowe, R. W. D. (1973). The ultrastructure of the Z discs from white, intermediate, and red fibers of mammalian striated muscles. J Cell Biol 57: 261.
66. Santhi D, Kalaikannan A, Sureshkumar S. (2017). Factors influencing meat emulsion properties and product texture: A review. Crit Rev Food Sci Nutr 57(10):2021-2027. doi: 10.1080/10408398.2013.858027.
67. Sarma, J., G. Reddy, V.S., Srikar, L.N. (2000). Effect of frozen storage on lipids and functional properties of proteins of dressed Indian oil sardine (Sardinella longiceps). Food Res Int 33: 815-820.
68. Savage, A.W.J., P.D. Warriss, P.D. Jolley. 1990. The amount and composition of the proteins in drip from stored pig meat. Meat Sci 27: 289-303.
69. Segura-Campos, M., Perez-Hernandez, R., ChelGurerero, L., Castellanos-Ruelas, A., GallegosThintore, S., Betancur-Ancona, D. (2013). Physicochemical and functional properties of dehydrated Japanese quail (Coturnix japonica) egg white. Food Nutr Sci 4: 289-298, doi: 10.4236/fns.2013.43039.
70. Sharifian, A., Soltanizadeh, N., Abbaszadeh, R. (2019). Effects of dielectric barrier discharge plasma on the physicochemical and functional properties of myofibrillar proteins. Innovative Food Sci Emerging Technol https://doi.org/10.1016/j.ifset.2019.03.006.
71. Shi, X., Zou, H., Sun, S. (2019). Application of high-pressure homogenization for improving the physicochemical, functional and rheological properties of myofibrillar protein. Int J Bio Macromol, https://doi.org/10.1016/j.ijbiomac.2019.07.110.
72. Siegel, D.G., Schmidt, G.R. (1979). Ionic, pH and temperature effects on the binding ability of myosin. J Food Sci 44:1686.
73. Smith, D.M. (1988). Meat proteins: functional properties in comminuted meat products, Food Technol 42 (4): 116–121.
74. Srikar, L. N., Vidya Sagar Reddy, G. (1991). Protein solubility and emulsifying capacity in frozen stored fish mince. J Sci Food Agric 55: 447-453.
75. Syska, H., Perry, S. V., Trayer, I. P. (1974). A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle. FEBS Lett 40, 253.
76. Takahashi, K., Hattori, A. (1989). α-Actinin is a component of the Z-filament, a structural backbone of skeletal muscle Z-disks. J Biochem (Tokyo), 105, 529.
77. Thawornchinsombut, S., Park, J.W., 2005. Role of ionic strength in biochemical properties of soluble fish proteins isolated from cryoprotected Pacific whiting mince. J Food Biochem 29(2): 132-151.
78. Theno, D.M., Siegel, D.G., Schmidt, G.R. (1978). Meat massaging: Effects of salt and phosphate on the ultrastructure of cured porcine muscle. J Food Sci 43: 488-492.
79. Torley, P.J., Young, O.A. (1995). Rheological changes during isothermal holding of salted beef homogenates. Meat Sci 39: 23-34.
80. Venugopal, V., Shahidi F. (1996). Structure and composition of fish muscle. Food Rev Int 12(2): 175-197, DOI: 10.1080/87559129609541074.
81. Visessanguan, W., Benjakul, S., Riebroy, S., Thepkasikul P. (2004). Changes in composition and functional properties of proteins and their contributions to nham characteristics. Meat Sci 66: 579-588.
82. Voutsinas, L.P., Cheung, E., Nakai, S. 1983. Relationships of hydrophobicity to emulsifying properties of heat denatured proteins. J Food Sci 48: 26–32.
83. Whiting, R.C. (1984), Stability and gel strength of frankfurter batters made with reduced NaCl. J Food Sci 49: 1350-1354. doi:10.1111/j.1365-2621.1984.tb14988.x
84. Wilding P, Hedges N, Lillford P. (1986). Salt-induced swelling of meat: the effect of storage time, pH, ion-type, and concentration. Meat Sci 18: 55–75.
85. Wu, F., Shi, X., Zou, H., Zhang, T., Dong, X., Zhu, R., Yu, C. (2019). Effects of high-pressure homogenization on physicochemical, rheological and emulsifying properties of myofibrillar protein. J Food Eng 263: 272–279.
86. Xiong, L., Blanchard, P. (1994). Myofibrillar protein gelation: Viscoelastic changes related to heating procedures. Kentucky Agric Experiment Station J 93‐6‐192.
87. Xiong, Y. L. (1994): Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing. Critical Rev Food Sci Nutrition 34(3): 293-320.
88. Xiong, Y.L., Blanchard, S.P. (1993). Viscoelastic properties of myofibrillar protein and polysaccharide composite gels. J Food Sci 58:164.
89. Xiong, Y.L., Brekke, C.J. (1991). Gelation properties of chicken myofibrils treated with calcium and magnesium chlorides. J Muscle Foods, 2: 21.
90. Xiong. Y.L. (1997). Structure-Function Relationship of Muscle Proteins. In Food Proteins and Their Applications; S. Damodaran and A. Paraf. Marcel Dekker: New York pp. 341-392.
91. Xiong, Y.L., Kenney P.B. (1999). Functionality of proteins in meat products. Reciprocal Meat Conference Proceedings, 52.
92. Xiong, Y.L., Lou, X., Wang, C., Moody, W.G., Harmon, R.J. (2000). Protein extraction from chicken myofibrils irrigated with various polyphosphate and NaCl solutions. J Food Sci 65: 96-100.
93. Yates, L. D., Greaser, M. L. (1983). Quantitative determination of myosin and actin in rabbit skeletal muscle. J Mol Biol 168, 123.
94. Yongsawatdigul J, Hemung BO. (2010). Structural changes and functional properties of threadfin bream sarcoplasmic proteins subjected to pH-shifting treatments and lyophilization. J Food Sci 75(3): 251-257. doi: 10.1111/j.1750-3841.2010.01530.x.
95. Young, O. A., Zhang, S. X., Farouk, M. M., Podmore, C. (2005). Effects of pH adjustment with phosphates on attributes and functionalities of normal and high pH beef. Meat Sci 70: 133–139.
96. Zeng, Z., Li, C., Ertbjerg, P. (2017). Relationship between proteolysis and water-holding of myofibrils. Meat Sci 131: 48– 55.
97. Zhang, L., Barbut, S. (2005). Rheological characteristics of fresh and frozen PSE, normal and DFD chicken breast meat, J Brit Poult Sci 46 : 687–693.
98. Zheng, J. et al., (2019). Partial substitution of NaCl with chloride salt mixtures: Impact on oxidative characteristics of meat myofibrillar protein and their rheological properties. Food Hydrocolloids 96: 36–42.
99. Zhou, L. et al., (2019). Effects of high-speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low-fat conditions. J Sci Food Agric 99: 6500–650.
100. Zouari, N., Fakhfakh, N., Amara-Dali, W. B., Sellami, M., Msaddak, L., Ayadi, M. A., (2011). Turkey liver: Physicochemical characteristics and functional properties of protein fractions. Food Bioprod Process 89: 142–148.