913
Views
22
CrossRef citations to date
0
Altmetric
Original Articles

Changes in Some Biochemical Indices of Stability of Broiler Chicken Actomyosin at Different Levels of Sodium Bicarbonate in Presence and Absence of Sodium Chloride

, &
Pages 1373-1384 | Received 18 Dec 2013, Accepted 21 Apr 2014, Published online: 09 Mar 2015

REFERENCES

  • Barbut, S.; Zhang, L.; Marcone, M. Effects of pale, normal, and dark chicken breast meat on microstructure, extractable proteins, and cooking of marinated fillets. Poultry Science 2005, 84 (5), 797–802.
  • Van Laack, R.L.; Liu, C.H.; Smith, M.O.; Loveday, H.D. Characteristics of pale, soft, exudative broiler breast meat. Poultry Science 2000, 79 (7), 1057–1061.
  • Fletcher, D.L. Poultry meat quality. World’s Poultry Science Journal 2002, 58, 131–145.
  • Xiong, Y.L.; Lou, X.; Wang, C.; Moody, W.G.; Harmon, R.J. Protein extraction from chicken myofibrils irrigated with various polyphosphate and NaCl solutions. Journal of Food Science 2000, 65 (1), 96–100.
  • Woelfel, R.L.; Sams, A.R. Marination performance of pale broiler breast meat. Poultry Science 2001, 80, 1519–1522.
  • Alvarado, C.Z.; Sams, A.R. Injection marination strategies for remediation of pale, exudative broiler breast meat. Poultry Science 2003, 82, 1332–1336.
  • Kauffman, R.G.; Van Laack, R.L.; Russell, R.L.; Pospiech, E.; Cornelius, C.A.; Suckow, C.E.; Greaser, M.L. Can pale, soft, exudative pork be prevented by postmortem sodium bicarbonate injection? Journal of Animal Science 1998, 76 (12), 3010–3015.
  • Wynveen, E.J.; Bowker, B.C.; Grant, A.L.; Lamkey, J.W.; Fennewald, K.J.; Henson, L.; Gerrard, D.E. Pork quality is affected by early postmortem phosphate and bicarbonate injection. Journal of Food Science 2001, 66 (6), 886–891.
  • Sen, A.R.; Naveena, B.M.; Muthukumar, M.; Babji, Y.; Murthy, T.R.K. Effect of chilling, polyphosphate, and bicarbonate on quality characteristics of broiler breast meat. British Poultry Science 2005, 46, 451–456.
  • Petracci, M.; Laghi, L.; Rocculi, P.; Rimini, S.; Panarese, V.; Cremonini, M.A.; Cavani, C. The use of sodium bicarbonate for marination of broiler breast meat. Poultry Science 2012, 91, 526–534.
  • Petracci, M.; Laghi, L.; Rimini, S.; Rocculi, P.; Capozzi, F.; Cavani, C. Chicken breast meat marinated with increasing levels of sodium bicarbonate. The Journal of Poultry Science 2013, DOI:http://dx.doi.org/10.2141/jpsa.0130079.
  • Xiong, Y.L.; Kupski, D.R. Time-dependent marinade absorption and retention, cooking yield, and palatability of chicken filets marinated in various phosphate solutions. Poultry Science 1999, 78, 1053–1059.
  • Lopez, K.; Schilling, M.W.; Armstrong, T.W.; Smith, B.S.; Corzo, A. Sodium chloride concentration affects yield, quality, and sensory acceptability of vacuum-tumbled marinated broiler breast fillets. Poultry science 2012, 91 (5), 1186–1194.
  • Acton, J.C.; Ziegler, G.R.; Burge, J.D.L.; Froning, G.W. Functionality of muscle constituents in the processing of comminuted meat products. Critical Reviews in Food Science and Nutrition 1982, 18 (2), 99–121.
  • Xiong, Y.L. Structure-function relationships of muscle proteins. Food Science and Technology-New York-Marcel Dekker 1997, 341–392.
  • Samejima, K.; Ishioroshi, M.; Yasui, T. Relative roles of the head and tail portions of the molecule in heat‐induced gelation of myosin. Journal of Food Science 1981, 46 (5), 1412–1418.
  • Cofrades, S.; Careche, M.; Carballo, J.; Colmenero, F.J. Freezing and frozen storage of actomyosin from different species. Zeitschrift für Lebensmittel-Untersuchung und Forschung 1996, 203, 316–319.
  • Bertram, H.C.; Kristensen, M.; Andersen, H.J. Functionality of myofibrillar proteins as affected by pH, ionic strength, and heat treatment—A low-field NM study. Meat Science 2004, 68, 249–256.
  • Xiang, D.S.; Holley, R.A. Factors influencing gel formation by myofibrillar proteins in muscle foods. Comprehensive Reviews in Food Safety 2011, 10, 33–51.
  • Ahmad, R.; Hasnain, A. Correlation between biochemical properties and adaptive diversity of skeletal muscle myofibrils and myosin of some air-breathing teleosts. Indian Journal of Biochemistry and Biophysics 2006, 43 (4), 217.
  • Lowry, O.H.; Rosebrough, N.J.; Farr, A.L.; Randall, R.J. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 1951, 193, 265–275.
  • Hasnain, A.; Samejima, K.; Takahashi, K.; Yasui, T. Molecular adaptability of carp myosin: A study of some physico-chemical properties and their comparison with those of rabbit myosin. Archives of Physiology and Biochemistry 1979, 87 (4), 643–662.
  • Fiske, C.H.; Subbarow, Y. The colorimetric determination of phosphorus. Journal of Biological Chemistry 1925, 66 (2), 375–400.
  • Ellman, G.L. Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics 1959, 82 (1), 70–77.
  • Ding, Y.; Wei-guo, S.; Yan, C. Comparative studies on the biochemical characteristics of natural actomyosin isolated from PSE and normal pork. Journal of Zhejiang University Science 2004, 5 (6), 684–688.
  • Liu, R.; Zhao, S.M.; Yang, H.; Li, D.D.; Xiong, S.B.; Xie, B.J. Comparative study on the stability of fish actomyosin and pork actomyosin. Meat Science 2011, 88 (2), 234–240.
  • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680–685.
  • Matsuura, M.; Arai, K. Effect of pH on filament-forming ability and biochemical activity of fish myosin. Nippon Suisan Gakkaishi 1986, 52 (9), 1657–1663.
  • Roura, S.I.; Crupkin, M. Biochemical and functional properties of myofibrils from pre- and post-spawned hake (Merluccius hubbsi marini) stored on ice. Journal of Food Science 1995, 60, 269–272.
  • Ahmad, R.; Hasnain, A. Peptide mapping of polymorphic myosin heavy chain isoforms in different muscle types of some freshwater teleosts. Fish Physiology and Biochemistry 2013, 39, 721–731.
  • Rayment, I. The structural basis of the myosin ATPase activity. Journal of Biological Chemistry 1996, 271 (27), 15850–15853.
  • Harrington, W.F.; Rodgers, M.E. Myosin. Annual review of biochemistry 1984, 53 (1), 35–73.
  • Warren, J.C., Stowring, L.; Morales, M.F. The effect of structure-disrupting ions on the activity of myosin and other enzymes. Journal of Biological Chemistry 1966, 241 (2), 309–316.
  • Yasui, T.; Gotoh, T.; Morita, J. Influence of pH and temperature on properties of myosin A in glycerol-treated fiber bundles. Journal of Agricultural and Food Chemistry 1973, 21 (2), 241–246.
  • Watabe, S.; Hashimoto, K.; Watanabe, S. The pH-dependency of myosin ATPases from yellowtail ordinary and dark muscles. Journal of Biochemistry 1983, 94 (6), 1867–1875.
  • Kawakami, H.; Morita, J.I.; Takahashi, K.; Yasui, T. Thermal denaturation of myosin, heavy meromyosin and subfragment-1. Journal of Biochemistry 1971, 70 (4), 635–648.
  • Sweeney, H.L. Function of the N terminus of the myosin essential light chain of vertebrate striated muscle. Biophysical Journal 1995, 68 (4 Suppl), 112S.
  • Ebashi, S. Regulatory mechanism of muscle contraction with special reference to the Ca-troponin-tropomyosin system. Essays in Biochemistry 1974, 10, 1.
  • Yu, L.P.; Lee, Y.B. Effects of postmortem pH and temperature muscle structure and meat tenderness. Journal of Food Science 1986, 51 (3), 774–780.
  • Wu, F.Y.; Smith, S.B. Ionic strength and myofibrillar protein solubilization. Journal of Animal Science 1987, 65 (2), 597–608.
  • Lan, Y.H.; Novakofski, J.; Carr, T.R.; McKeith, F.K. Assay and storage conditions affect yield of salt soluble protein from muscle. Journal of Food Science 1993, 58 (5), 963–967.
  • Chang, H.S.; Hultin, H.O.; Dagher, S.M. Effect of MgCl2/sodium pyrophosphate on chicken breast muscle myosin solubilization and gelation. Journal of Food Biochemistry 2001, 25 (5), 459–474.
  • Wang, S.F.; Smith, D.M. Gelation of chicken breast muscle actomyosin as influenced by weight ratio of actin to myosin. Journal of Agricultural and Food Chemistry 1995, 43 (2), 331–336.
  • Xiong, Y.L.; Lou, X.; Harmon, R.J.; Wang, C.; Moody, W.G. Salt- and pyrophosphate-induced structural changes in myofibrils from chicken red and white muscles. Journal of Science and Food Agriculture 2000, 80, 1176–1182.
  • Chantarasuwan, C.; Benjakul, S.; Visessanguan, W. The effects of sodium bicarbonate on conformational changes of natural actomyosin from Pacific white shrimp (Litopenaeus vannamei). Food Chemistry 2011, 129, 1636–1643.
  • Pietrzak, M.; Greaser, M.L.; Sosnicki, A.A. Effect of rapid rigor mortis processes on protein functionality in pectoralis major muscle of domestic turkeys. Journal of Animal Science 1997, 75 (8), 2106–2116.
  • Bertram, H.C.; Meyer, R.L.; Wu, Z.; Zhou, X.; Andersen, H.J. Water distribution and microstructure in enhanced structure in pork. Journal of Agricultural and Food Chemistry 2008, 56 (16), 7201–7207.
  • Yasui, T.; Ishioroshi, M.; Samejima, K. Effect of actomyosin on heat gelation of myosin. Agricultural and Biological Chemistry 1982, 46 (4), 1049–1059.
  • Mohan, M.; Ramachandran, D.; Sankar, T.V.; Anandan, R. Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus). Process Biochemistry 2007, 42 (7), 1056–1062.
  • Wen-Ching, K.; Yu, C.C.; Hsu, K.C. Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment. LWT-Food Science and Technology 2007, 40 (8), 1316–1320.
  • Benjakul, S.; Visessanguan, W.; Ishizaki, S., Tanaka, M. Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus, and Priacanthus macracanthus. Journal of Food Science 2001, 66 (9), 1311–1318.
  • Tein, L.M.; Jae, W.P. Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. Journal of Food Science 1998, 63 (2). 215–218.
  • Smyth, A.B.; Smith, D.M.; O’Neill, E. Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin. Journal of Food Science 1998, 63 (4), 584–587.
  • Lymn, R.W.; Taylor, E.W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 1971, 10 (25), 4617–4624.
  • Juan, Y.; Pan, J.; Shen, H.; Luo, Y. Changes in physicochemical properties of bighead carp (Aristichthys mobilis) actomyosin by thermal treatment. International Journal of Food Properties 2012, 15 (6), 1276–1285.
  • Mothershaw, A.N.; Gaffer, T.; Kadim, I.; Guizani, N.; Al-Amri, I.; Mahgoub, O.; Al-Bahry S. Quality characteristics of broiler chicken meat on salt at different temperatures. International Journal of Food Properties 2009, 12 (3), 681–690.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.