Solubilization of myofibrillar proteins in water or low ionic strength media: Classical techniques, basic principles, and novel functionalities

References

• Alarcon-Rojo, A., Janacua, H., Rodriguez, J., Paniwnyk, L. and Mason, T. (2015). Power ultrasound in meat processing. Meat Sci. 107:86–93.
   PubMed Web of Science ®Google Scholar
• Bailey, A. J. and Light, N. D. (1989). Connective tissue in meat and meat products. Elsevier Applied Science, Barking, England.
   Google Scholar
• Bandman, E. (1999). Solubility of myosin and the binding quality of meat products. Int. Congr Meat Sci Technol. 45:236–245.
   Google Scholar
• Bandman, E., Arrizubieta, M.J., Wick, M., Hattori, A., Tablin, F., Zhang, S. and Zhang, Q. (1997). Functional analysis of the chicken sarcomeric myosin rod: Regulation of dimerization, solubility, and fibrillogenesis. Cell Struct. Funct. 22(1):131–137.
   PubMed Web of Science ®Google Scholar
• Banga, I. and Szent-Györgyi, A. (1942). Preparation and properties of myosin A and B. Stud. Inst. Med. Chem. Univ. Szeged. I:5–15.
   Google Scholar
• Boland, M. J., Rae, A. N., Vereijken, J. M., Meuwissen, M. P., Fischer, A. R., van Boekel, M. A., Rutherfurd, S. M., Gruppen, H., Moughan, P. J. and Hendriks, W. H. (2013). The future supply of animal-derived protein for human consumption. Trends Food Sci. Tech. 29(1):62–73.
   Web of Science ®Google Scholar
• Bouton, P., Ford, A., Harris, P., Macfarlane, J. and O'shea, J. (1977). Pressure-heat treatment of post rigor muscle: Effects on tenderness. J. Food Sci. 42(1):132–135.
   Web of Science ®Google Scholar
• Buckow, R., Sikes, A. and Tume, R. (2013). Effect of high pressure on physicochemical properties of meat. Crit. Rev. Food Sci. 53(7):770–786.
   PubMed Web of Science ®Google Scholar
• Chang, H. S. (1997). Solubility and gelation of chicken breast muscle proteins as affected by salts. Doctoral Dissertations Available from Proquest Paper AAI9721436.
   Google Scholar
• Chang, H. S., Feng, Y. and Hultin, H. O. (2001). Role of pH in gel formation of washed chicken muscle at low ionic strength. J. Food Biochem. 25(5):439–457.
   Web of Science ®Google Scholar
• Cheah, P. and Ledward, D. (1996). High pressure effects on lipid oxidation in minced pork. Meat Sci. 43(2):123–134.
   PubMed Web of Science ®Google Scholar
• Cheftel, J. C. and Culioli, J. (1997). Effects of high pressure on meat: A review. Meat Sci. 46(3):211–236.
   PubMed Web of Science ®Google Scholar
• Chen, Y. C. and Jaczynski, J. (2007). Protein recovery from rainbow trout (Oncorhynchus mykiss) processing byproducts via isoelectric solubilization/precipitation and its gelation properties as affected by functional additives. J. Agric. Food Chem. 55(22):9079–9088.
   PubMed Web of Science ®Google Scholar
• Cho, Y. J., Lee, N. H., Yang, S. Y., Kim, Y. B., Kim, Y. H., Lim, S. D., Jeon, K. H. and Kim, K. S. (2007). Effects of sonication on the water-solubilization of myofibrillar proteins from breast muscle of spent hen. Kor. J. Food Sci. An. 27(4):457–462.
   Web of Science ®Google Scholar
• Choi, Y. J. and Park, J. W. (2002). Acid‐aided protein recovery from enzyme‐rich pacific whiting. J. Food Sci. 67(8):2962–2967.
   Web of Science ®Google Scholar
• Chou, Y. T. and Lin, K. W. (2010). Effects of xylooligosaccharides and sugars on the functionality of porcine myofibrillar proteins during heating and frozen storage. Food Chem. 121(1):127–131.
   Web of Science ®Google Scholar
• Craig, R. and Woodhead, J. L. (2006). Structure and function of myosin filaments. Curr. Opin. Struc. Biol. 16(2):204–212.
   PubMed Web of Science ®Google Scholar
• Dagher, S. M., Hultin, H. O. and Liang, Y. (2000). Solubility of cod muscle myofibrillar proteins at alkaline pH. J. Aquat. Food Prod. T. 9(4):49–59.
   Google Scholar
• Dutson, T. R., Pearson, A. M., Merkel, R. A. and Spink, G. C. (1974). Ultrastructural postmortem changes in normal and low quality porcine muscle fibers. J. Food Sci. 39(1):32–37.
   Web of Science ®Google Scholar
• Fürst, D. O., Osborn, M., Nave, R. and Weber, K. (1988). The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J. Cell Biol. 106(5):1563–1572.
   PubMed Web of Science ®Google Scholar
• Feng, Y. and Hultin, H. O. (1997). Solubility of the proteins of mackerel light muscle at low ionic strength. J. Food Biochem. 21(1):479–496.
   Web of Science ®Google Scholar
• Feng, Y. and Hultin, H. O. (2001). Effect of pH on the rheological and structural properties of gels of water-washed chicken-breast muscle at physiological ionic strength. J. Agric. Food Chem. 49(8):3927–3935.
   PubMed Web of Science ®Google Scholar
• Foh, M. B. K., Wenshui, X., Amadou, I. and Jiang, Q. (2012). Influence of pH shift on functional properties of protein isolated of tilapia (Oreochromis niloticus) muscles and of soy protein isolate. Food Bioprocess Tech. 5(6):2192–2200.
   Web of Science ®Google Scholar
• Gülseren, İ., Güzey, D., Bruce, B. D. and Weiss, J. (2007). Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrason. Sonochem. 14(2):173–183.
   PubMed Web of Science ®Google Scholar
• Gehring, C. K., Gigliotti, J. C., Moritz, J. S., Tou, J. C. and Jaczynski, J. (2011). Functional and nutritional characteristics of proteins and lipids recovered by isoelectric processing of fish by-products and low-value fish: A review. Food Chem. 124(2):422–431.
   Web of Science ®Google Scholar
• Ghosh, T., García, A. E. and Garde, S. (2001). Molecular dynamics simulations of pressure effects on hydrophobic interactions. J. Am. Chem. Soc. 123(44):10997–11003.
   PubMed Web of Science ®Google Scholar
• Goll, D. E., Neti, G., Mares, S. W. and Thompson, V. F. (2008). Myofibrillar protein turnover: The proteasome and the calpains. J. Anim. Sci. 86(14 Suppl):E19–35.
   PubMedGoogle Scholar
• Gross, M. and Jaenicke, R. (1994). Proteins under pressure. Eur. J. Biochem. 221(2):617–630.
   PubMedGoogle Scholar
• Guo, X. Y., Peng, Z. Q., Zhang, Y. W., Liu, B. and Cui, Y. Q. (2015). The solubility and conformational characteristics of porcine myosin as affected by the presence of L-lysine and L-histidine. Food Chem. 170:212–217.
   PubMed Web of Science ®Google Scholar
• Harano, Y. and Kinoshita, M. (2006). On the physics of pressure denaturation of proteins. J. Phys-Condens. Mat. 18(7):L107.
   Web of Science ®Google Scholar
• Harano, Y., Yoshidome, T. and Kinoshita, M. (2008). Molecular mechanism of pressure denaturation of proteins. J. Chem. Phys. 129(14):145103.
   PubMed Web of Science ®Google Scholar
• Hay, J. D., Currie, R. W., Wolfe, F. H. and Sanders, E. J. (1973). Effect of postmortem aging on chicken muscle fibrils. J. Food Sci. 38(6):981–986.
   Web of Science ®Google Scholar
• Hayakawa,  , Ito, T., Wakamatsu, J., Nishimura, T. and Hattori, A. (2009). Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine. Meat Sci. 82(2):151–154.
   PubMed Web of Science ®Google Scholar
• Hayakawa,  , Ito, T., Wakamatsu, J., Nishimura, T. and Hattori, A. (2010). Myosin filament depolymerizes in a low ionic strength solution containing L-histidine. Meat Sci. 84(4):742–746.
   PubMed Web of Science ®Google Scholar
• Hayakawa,  , Yoshida, Y., Yasui, M., Ito, T., Iwasaki, T., Wakamatsu, J., Hattori, A. and Nishimura, T. (2012). Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine. Meat Sci. 90(1):77–80.
   PubMed Web of Science ®Google Scholar
• Hermansson, A. M., Harbitz, O. and Langton, M. (1986). Formation of two types of gels from bovine myosin. J. Sci. Food Agr. 37(1):69–84.
   Web of Science ®Google Scholar
• Hrynets, Y., Ndagijimana, M. and Betti, M. (2014). Transglutaminase-catalyzed glycosylation of natural actomyosin (NAM) using glucosamine as amine donor: Functionality and gel microstructure. Food Hydrocolloids. 36:26–36.
   Web of Science ®Google Scholar
• Hrynets, Y., Omana, D. A., Xu, Y. and Betti, M. (2010). Effect of acid‐and alkaline‐aided extractions on functional and rheological properties of proteins recovered from mechanically separated turkey meat (MSTM). J. Food Sci. 75(7):E477–E486.
   PubMed Web of Science ®Google Scholar
• Hrynets, Y., Omana, D. A., Xu, Y. and Betti, M. (2011). Comparative study on the effect of acid-and alkaline-aided extractions on mechanically separated turkey meat (MSTM): Chemical characteristics of recovered proteins. Process Biochem. 46(1):335–343.
   Web of Science ®Google Scholar
• Hu, H., Wu, J., Li-Chan, E. C., Zhu, L., Zhang, F., Xu, X., Fan, G., Wang, L., Huang, X. and Pan, S. (2013). Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids. 30(2):647–655.
   Web of Science ®Google Scholar
• Huff-Lonergan, E. and Lonergan, S. M. (2005). Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci. 71(1):194–204.
   PubMed Web of Science ®Google Scholar
• Huhin, H. O. and Kelleher, S. D. (1999). Process for isolating a protein composition from a muscle source and protein composition. U.S. Patent No. 6005,073.
   Google Scholar
• Hultin, H. O., Feng, Y. and Stanley, D. W. (1995). A re‐examination of muscle protein solubility. J. Muscle Foods. 6(2):91–107.
   Google Scholar
• Hultin, H. O. and Kelleher, S. (2002). Protein composition and process for isolating a protein composition from a muscle source. U.S. Patent No. 6451,975.
   Google Scholar
• Hultin, H. O. and Kelleher, S. D. (2000). High efficiency alkaline protein extraction. U.S.Patent No. 6136,959.
   Google Scholar
• Hummer, G., Garde, S., García, A. E., Paulaitis, M. E. and Pratt, L. R. (1998). The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl. Acad. Sci. 95(4):1552–1555.
   PubMed Web of Science ®Google Scholar
• Ikkai, T. and Ooi, T. (1966). The effects of pressure on FG transformation of actin.Biochem. 5(5):1551–1560.
   PubMed Web of Science ®Google Scholar
• Ingadottir, B. and Kristinsson, H. G. (2010). Gelation of protein isolates extracted from tilapia light muscle by pH shift processing. Food Chem. 118(3):789–798.
   Web of Science ®Google Scholar
• Ishioroshi, M., Jima, K. S. and Yasui, T. (1979). Heat‐induced gelation of myosin: Factors of pH and salt concentrations. J. Food Sci. 44(5):1280–1284.
   Web of Science ®Google Scholar
• Ito, Y., Tatsumi, R., Wakamatsu, J. I., Nishimura, T. and Hattori, A. (2003). The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water. Anim. Sci. J. 74(5):417–425.
   Google Scholar
• Ito, Y., Toki, S., Omori, T., Ide, H., Tatsumi, R., Wakamatsu, J.i., Nishuimura, T. and Hattori, A. (2004). Physicochemical properties of water‐soluble myofibrillar proteins prepared from chicken breast muscle. Anim. Sci. J. 75(1):59–65.
   Google Scholar
• Jambrak, A. R., Mason, T. J., Lelas, V., Herceg, Z. and Herceg, I. L. (2008). Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. J. Food Eng. 86(2):281–287.
   Web of Science ®Google Scholar
• James, J. M. and DeWitt, C. A. (2004). Gel attributes of beef heart when treated by acid solubilization isoelectric precipitation. J. Food Sci. 69(6):C473–C479.
   Web of Science ®Google Scholar
• Jung, S., de Lamballerie-Anton, M. and Ghoul, M. (2000). Modifications of ultrastructure and myofibrillar proteins of post-rigor beef treated by high pressure. LWT-Food Sci.Technol. 33(4):313–319.
   Web of Science ®Google Scholar
• Kaminer, B. and Bell, A. L. (1966). Myosin filamentogenesis: Effects of pH and ionic concentration. J. Mol. Biol. 20(2):391–401.
   PubMed Web of Science ®Google Scholar
• Katayama, S., Haga, Y. and Saeki, H. (2004). Loss of filament-forming ability of myosin by non-enzymatic glycosylation and its molecular mechanism. FEBS Lett. 575(1):9–13.
   PubMed Web of Science ®Google Scholar
• Katayama, S. and Saeki, H. (2004). Cooperative effect of relative humidity and glucose concentration on improved solubility of shellfish muscle protein by the Maillard reaction. Fisheries Sci. 70(1):159–166.
   Web of Science ®Google Scholar
• Katayama, S. and Saeki, H. (2007). Water solubilization of glycated carp and scallop myosin rods, and their soluble state under physiological conditions. Fisheries Sci. 73(2):446–452.
   Web of Science ®Google Scholar
• Katayama, S., Shima, J. and Saeki, H. (2002). Solubility improvement of shellfish muscle proteins by reaction with glucose and its soluble state in low-ionic-strength medium. J. Agric. Food Chem. 50(15):4327–4332.
   PubMed Web of Science ®Google Scholar
• Ke, S. and Hultin, H. O. (2005). Role of reduced ionic strength and low pH in gelation of chicken breast muscle protein. J. Food Sci. 70(1):E1–E6.
   Web of Science ®Google Scholar
• Kelleher, S. D. (2000). Physical characteristics of muscle protein extracts prepared using low ionic strength, acid solubilization/precipitation. Doctoral Dissertations Available from Proquest.Paper AAI9988808.
   Google Scholar
• Kelleher, S. D., Feng, Y., Hultin, H. O. and Livingston, M. B. (2004). Role of initial muscle pH on the solubility of fish muscle proteins in water. J. Food Biochem. 28(4):279–292.
   Web of Science ®Google Scholar
• Khiari, Z., Pietrasik, Z., Gaudette, N. J. and Betti, M. (2014). Poultry protein isolate prepared using an acid solubilization/precipitation extraction influences the microstructure, the functionality and the consumer acceptability of a processed meat product. Food Struct. 2(1):49–60.
   Google Scholar
• Korzeniowska, M., Cheung, I. W. Y. and Li-Chan, E. C. Y. (2013). Effects of fish protein hydrolysate and freeze–thaw treatment on physicochemical and gel properties of natural actomyosin from Pacific cod. Food Chem. 138(2):1967–1975.
   PubMed Web of Science ®Google Scholar
• Krishnamurthy, G., Chang, H. S., Hultin, H. O., Feng, Y., Srinivasan, S. and Kelleher, S. D. (1996). Solubility of chicken breast muscle proteins in solutions of low ionic strength. J. Agric. Food Chem. 44(2):408–415.
   Web of Science ®Google Scholar
• Kristinsson, H. G. and Hultin, H. O. (2003a). Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J. Agric. Food Chem. 51(24):7187–7196.
   PubMed Web of Science ®Google Scholar
• Kristinsson, H. G. and Hultin, H. O. (2003b). Effect of low and high pH treatment on the functional properties of cod muscle proteins. J. Agric. Food Chem. 51(17):5103–5110.
   PubMed Web of Science ®Google Scholar
• Labeit, S. and Kolmerer, B. (1995). Titins: Giant proteins in charge of muscle ultrastructure and elasticity. Science. 270(5234):293–296.
   PubMed Web of Science ®Google Scholar
• Lee, S. H., Joo, S. T. and Ryu, Y. C. (2010). Skeletal muscle fiber type and myofibrillar proteins in relation to meat quality. Meat Sci. 86(1):166–170.
   PubMed Web of Science ®Google Scholar
• Liang, Y. and Hultin, H. O. (2003). Functional protein isolates from mechanically deboned turkey by alkaline solubilization with isoelectric precipitation. J. Muscle Foods. 14(3):195–205.
   Web of Science ®Google Scholar
• Lin, T. M. and Park, J. W. (1998). Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. J. Food Sci. 63(2):215–218.
   Web of Science ®Google Scholar
• Liu, J., Ru, Q. and Ding, Y. (2012). Glycation a promising method for food protein modification: Physicochemical properties and structure, a review. Food Res. Int. 49(1):170–183.
   Web of Science ®Google Scholar
• Ma, H., Zhou, G., Ledward, D. A., Yu, X. and Pan, R. (2011). Effect of combined high pressure and thermal treatment on myofibrillar proteins solubilization of beef muscle. Int. J. Mol. Sci. 12(5):3034–3041.
   PubMed Web of Science ®Google Scholar
• Macfarlane, J. (1974). Pressure‐induced solubilization of meat proteins in saline solution. J. Food Sci. 39(3):542–547.
   Web of Science ®Google Scholar
• Macfarlane, J. and McKenzie, I. (1976). Pressure‐induced solubilization of myofibrillar proteins. J. Food Sci. 41(6):1442–1446.
   Web of Science ®Google Scholar
• Maitena, U., Katayama, S., Sato, R. and Saeki, H. (2004). Improved solubility and stability of carp myosin by conjugation with alginate oligosaccharide. Fisheries Sci. 70(5):896–902.
   Web of Science ®Google Scholar
• Marcos, B. and Mullen, A. M. (2014). High pressure induced changes in beef muscle proteome: Correlation with quality parameters. Meat Sci. 97(1):11–20.
   PubMed Web of Science ®Google Scholar
• Marmon, S. K., Krona, A., Langton, M. and Undeland, I. (2012). Changes in salt solubility and microstructure of proteins from herring (Clupea harengus) after pH-shift processing. J. Agric. Food Chem. 60(32):7965–7972.
   PubMed Web of Science ®Google Scholar
• Marmon, S. K. and Undeland, I. (2013). Effect of alkaline pH-shift processing on in vitro gastrointestinal digestion of herring (Clupea harengus) fillets. Food Chem. 138(1):214–219.
   PubMed Web of Science ®Google Scholar
• Maruyama, K. (1997). Connectin/titin, giant elastic protein of muscle. FASEB J. 11(5):341–345.
   PubMed Web of Science ®Google Scholar
• Matak, K. E., Tahergorabi, R. and Jaczynski, J. (2015). A review: Protein isolates recovered by isoelectric solubilization/precipitation processing from muscle food by-products as a component of nutraceutical foods. Food Res. Int. 77:697–703.
   Web of Science ®Google Scholar
• Mireles DeWitt, C. A., Nabors, R. L. and Kleinholz, C. W. (2007). Pilot plant scale production of protein from catfish treated by acid solubilization/isoelectric precipitation.J. Food Sci. 72(6):E351–E355.
   PubMed Web of Science ®Google Scholar
• Mohan, M., Ramachandran, D., Sankar, T. V. and Anandan, R. (2007). Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus). Process Biochem. 42(7):1056–1062.
   Web of Science ®Google Scholar
• Moos, C., Mason, C. M., Besterman, J. M., Feng, I.N. M. and Dubin, J. H. (1978). The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1.J. Mol. Biol. 124(4):571–586.
   PubMed Web of Science ®Google Scholar
• Nakasawa, T., Takahashi, M., Matsuzawa, F., Aikawa, S., Togashi, Y., Saitoh, T., Yamagishi, A. and Yazawa, M. (2005). Critical regions for assembly of vertebrate nonmuscle myosin II. Biochem. 44(1):174–183.
   PubMed Web of Science ®Google Scholar
• Nayak, R., Kenney, P. B. and Slider, S. (1996). Protein extractability of turkey breast and thigh muscle with varying sodium chloride solutions as affected by calcium, magnesium and zinc chloride. J. Food Sci. 61(6):1149–1154.
   Web of Science ®Google Scholar
• Nieuwenhuizen, W. F., Weenen, H., Rigby, P. and Hetherington, M. M. (2010). Older adults and patients in need of nutritional support: Review of current treatment options and factors influencing nutritional intake. Clin.Nutr. 29(2):160–169.
   PubMed Web of Science ®Google Scholar
• Nishimura, K., Murakoshi, M., Katayama, S. and Saeki, H. (2010). Changes in solubility and thermal stability of chicken myofibrillar protein by glycosylation. Food Sci. Technol. Res. 17(1):69–75.
   Web of Science ®Google Scholar
• Nishimura, K., Murakoshi, M., Katayama, S. and Saeki, H. (2011). Antioxidative ability of chicken myofibrillar protein developed by glycosylation and changes in the solubility and thermal stability. Biosci.Biotechnol.Biochem. 75(2):247–254.
   PubMed Web of Science ®Google Scholar
• Nolsøe, H. and Undeland, I. (2009). The acid and alkaline solubilization process for the isolation of muscle proteins: State of the art. Food Bioprocess Tech. 2(1):1–27.
   Web of Science ®Google Scholar
• Nurkhoeriyati, T., Huda, N. and Ahmad, R. (2011). Gelation properties of spent duck meat surimi‐like material produced using acid–alkaline solubilization methods. J. Food Sci. 76(1):S48–S55.
   PubMed Web of Science ®Google Scholar
• Obermann, W. M. J., van der Ven, P. F. M., Steiner, F., Weber, K. and Fürst, D. O. (1998). Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band. Mol. Biol. Cell. 9(4):829–840.
   PubMed Web of Science ®Google Scholar
• Offer, G. and Trinick, J. (1983). On the mechanism of water holding in meat: The swelling and shrinking of myofibrils. Meat Sci. 8(4):245–281.
   PubMed Web of Science ®Google Scholar
• Oliveira, F. C.d., Coimbra, J. S. d. R., de Oliveira, E. B., Zuñiga, A. D. G. and Rojas, E. E. G. (2016). Food protein-polysaccharide conjugates obtained via the Maillard reaction: A review. Crit. Rev. Food Sci. 57(7):1108–1125.
   Web of Science ®Google Scholar
• Omana, D. A., Xu, Y., Moayedi, V. and Betti, M. (2010). Alkali-aided protein extraction from chicken dark meat: Chemical and functional properties of recovered proteins. Process Biochem. 45(3):375–381.
   Web of Science ®Google Scholar
• Özyurt, G., Şimşek, A., Karakaya, B. T., Aksun, E. T. and Yeşilsu, A. F. (2015). Functional, physicochemical and nutritional properties of protein from Klunzinger's ponyfish extracted by the pH shifting method. J. Food Process. Pres. 39(6):1934–1943.
   Web of Science ®Google Scholar
• Pérez-Mateos, M., Amato, P. M. and Lanier, T. C. (2004). Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization. J. Food Sci. 69(4):FCT328–FCT333.
   Web of Science ®Google Scholar
• Paker, I., Beamer, S., Jaczynski, J. and Matak, K. E. (2015). pH shift protein recovery with organic acids on texture and color of cooked gels. J. Sci. Food Agr. 95(2):275–280.
   PubMed Web of Science ®Google Scholar
• Parsons, N. and Knight, P. (1990). Origin of variable extraction of myosin from myofibrils treated with salt and pyrophosphate. J. Sci. Food Agr. 51(1):71–90.
   Web of Science ®Google Scholar
• Pearce, K. L., Rosenvold, K., Andersen, H. J. and 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(2):111–124.
   PubMed Web of Science ®Google Scholar
• Pereira, P. M. and Vicente, A. F. (2013). Meat nutritional composition and nutritive role in the human diet. Meat Sci. 93(3):586–592.
   PubMed Web of Science ®Google Scholar
• Raghavan, S. and Kristinsson, H. G. (2007). Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding. J. Agric. Food Chem. 55(10):4144–4153.
   PubMed Web of Science ®Google Scholar
• Raghavan, S. and Kristinsson, H. G. (2008). Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding. Food Chem. 107(1):385–398.
   Web of Science ®Google Scholar
• Reed, Z. H. and Park, J. W. (2011). Thermophysical characterization of tilapia myosin and its subfragments. J. Food Sci. 76(7):C1050–C1055.
   PubMed Web of Science ®Google Scholar
• Saeki, H. (1997). Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose: Biochemical properties and emulsifying properties. J. Agric. Food Chem. 45(3):680–684.
   Web of Science ®Google Scholar
• Saeki, H. (2010). A new approach to the functional improvement of fish meat proteins. In: Handbook of Seafood Quality, Safety and Health Applications, pp. 380–389.Cesarettin, A., Kazuo, M., Fereidoon, S. and Udaya, W., Eds. John Wiley, New York.
   Google Scholar
• Saeki, H. (2012). Protein–saccharide interaction. In: Food Proteins and Peptides: Chemistry, Functionality, Interactions, and Commercialization, pp. 230–253, Hettiarachchy, N. S., Sato, K., Marshall, M. R. and Kannan, A., Eds.
   Google Scholar
• Saeki, H. and Inoue, K. (1997). Improved solubility of carp myofibrillar proteins in low ionic strength medium by glycosylation. J. Agric. Food Chem. 45(9):3419–3422.
   Web of Science ®Google Scholar
• Saeki, H. and Tanabe, M. (1999). Change in solubility of carp myofibrillar protein by glycosylation with ribose. Fisheries Sci. 65(6):967–968.
   Web of Science ®Google Scholar
• Saleem, R., Hasnain, A., Ahmad, R. and Yildiz, F. (2015). Solubilisation of muscle proteins from chicken breast muscle by ultrasonic radiations in physiological ionic medium. Cogent Food Agr. 1(1):1046716.
   Google Scholar
• Sanmartín, E., Arboleya, J. C., Villamiel, M. and Moreno, F. J. (2009). Recent advances in the recovery and improvement of functional proteins from fish processing by‐products: Use of protein glycation as an alternative method. Compr. Rev. Food Sci. F. 8(4):332–344.
   Web of Science ®Google Scholar
• Sato, R., Katayama, S., Sawabe, T. and Saeki, H. (2003). Stability and emulsion-forming ability of water-soluble fish myofibrillar protein prepared by conjugation with alginate oligosaccharide. J. Agric. Food Chem. 51(15):4376–4381.
   PubMed Web of Science ®Google Scholar
• Sato, R., Sawabe, T., Kishimura, H., Hayashi, K. and Saeki, H. (2000). Preparation of neoglycoprotein from carp myofibrillar protein and alginate oligosaccharide: Improved solubility in low ionic strength medium. J. Agric. Food Chem. 48(1):17–21.
   PubMed Web of Science ®Google Scholar
• Sato, R., Sawabe, T. and Saeki, H. (2005). Characterization of fish myofibrillar protein by conjugation with alginate oligosaccharide prepared using genetic recombinant alginate lyase. J. Food Sci. 70(1):C58–C62.
   Web of Science ®Google Scholar
• Sikes, A., Tobin, A. and Tume, R. (2009). Use of high pressure to reduce cook loss and improve texture of low-salt beef sausage batters. Innov. Food Sci. Emerg. 10(4):405–412.
   Web of Science ®Google Scholar
• Sikes, A., Tornberg, E. and Tume, R. (2010). A proposed mechanism of tenderising post-rigor beef using high pressure–heat treatment. Meat Sci. 84(3):390–399.
   PubMed Web of Science ®Google Scholar
• Silva, J. L., Oliveira, A. C., Vieira, T. C., de Oliveira, G. A., Suarez, M. C. and Foguel, D. (2014). High-pressure chemical biology and biotechnology. Chem. Rev. 114(14):7239–7267.
   PubMed Web of Science ®Google Scholar
• Sinard, J. H., Stafford, W. F. and Pollard, T. D. (1989). The mechanism of assembly of acanthamoeba myosin-II minifilaments: Minifilaments assemble by three successive dimerization steps. J. Cell Biol. 109(4):1537–1547.
   PubMed Web of Science ®Google Scholar
• Sohn, R. L., Vikstrom, K. L., Strauss, M., Cohen, C., Szent-Gyorgyi, A. G. and Leinwand, L. A. (1997). A 29 residue region of the sarcomeric myosin rod is necessary for filament formation. J. Mol. Biol. 266(2):317–330.
   PubMed Web of Science ®Google Scholar
• Stanley, D. W., Stone, A. P. and Hultin, H. O. (1994). Solubility of beef and chicken myofibrillar proteins in low ionic strength media.J. Agric. Food Chem. 42(4):863–867.
   Web of Science ®Google Scholar
• Stefansson, G. and Hultin, H. O. (1994). On the solubility of cod muscle proteins in water. J. Agric. Food Chem. 42(12):2656–2664.
   Web of Science ®Google Scholar
• Straub, F. (1943). Actin, II. Stud. Inst. Med. Chem. Univ. Szeged. 3:23–37.
   Google Scholar
• Sun, X. D. and Holley, R. A. (2011). Factors influencing gel formation by myofibrillar proteins in muscle foods. Compr. Rev. Food Sci. F. 10(1):33–51.
   Web of Science ®Google Scholar
• Szent-Györgyi, A. (1943). The crystallization of myosin and some of its properties and reactions. Stud. Inst. Med. Chem. Univ. Szeged. 3:76–85.
   Google Scholar
• Tahergorabi, R., Beamer, S. K., Matak, K. E., and Jaczynski, J. (2011). Effect of isoelectric solubilization/precipitation and titanium dioxide on whitening and texture of proteins recovered from dark chicken-meat processing by-products. LWT-Food Sci. Technol. 44(4):896–903.
   Web of Science ®Google Scholar
• Tahergorabi, R. and Jaczynski, J. (2014). Isoelectric solubilization/precipitation as a means to recover protein and lipids from seafood by-products. In: Seafood Processing by-Products, pp. Kim, S. K., Perera, U., Rajapakse, N. and Kim, S. Eds. Springer, New York.
   Google Scholar
• Tahergorabi, R., Matak, K. E. and Jaczynski, J. (2015). Fish protein isolate: Development of functional foods with nutraceutical ingredients. J. Funct. Foods. 18:746–756.
   Web of Science ®Google Scholar
• Tahergorabi, R., Sivanandan, L. and Jaczynski, J. (2012). Dynamic rheology and endothermic transitions of proteins recovered from chicken-meat processing by-products using isoelectric solubilization/precipitation and addition of TiO2. LWT-Food Sci.Technol. 46(1):148–155.
   Web of Science ®Google Scholar
• Takahashi, K. and Hattori, A. (1989). α-Actinin is a component of the Z-filament, a structural backbone of skeletal muscle Z-disks. J. Biochem. 105(4):529–536.
   PubMed Web of Science ®Google Scholar
• Takai, E., Yoshizawa, S., Ejima, D., Arakawa, T. and Shiraki, K. (2013). Synergistic solubilization of porcine myosin in physiological salt solution by arginine.Int. J. Biol. Macromol. 62:647–651.
   PubMed Web of Science ®Google Scholar
• Takeda, H., Iida, T., Okada, A., Ootsuka, H., Ohshita, T., Masutani, E., Katayama, S. and Saeki, H. (2007). Feasibility study on water solubilization of spawned out salmon meat by conjugation with alginate oligosaccharide. Fisheries Sci. 73(4):924–930.
   Web of Science ®Google Scholar
• Tanabe, M. and Saeki, H. (2001). Effect of Maillard reaction with glucose and ribose on solubility at low ionic strength and filament-forming ability of fish myosin.J. Agric. Food Chem. 49(7):3403–3407.
   PubMed Web of Science ®Google Scholar
• Taylor, R. G., Geesink, G. H., Thompson, V. F., Koohmaraie, M. and Goll, D. E. (1995). Is Z-sisk degradation responsible for postmortem tenderization? J. Anim. Sci. 73:1351–1367.
   PubMed Web of Science ®Google Scholar
• Thawornchinsombut, S. and Park, J. W. (2004). Role of pH in solubility and conformational changes of Pacific whiting muscle proteins. J. Food Biochem. 28(2):135–154.
   Web of Science ®Google Scholar
• Tian, J., Wang, Y., Zhu, Z., Zeng, Q. and Xin, M. (2015). Recovery of tilapia (oreochromis niloticus) protein isolate by high-intensity ultrasound-aided alkaline isoelectric solubilization/precipitation process. Food Bioprocess Tech. 8(4):758–769.
   Web of Science ®Google Scholar
• Tokifuji, A., Matsushima, Y., Hachisuka, K. and Yoshioka, K. (2013). Texture, sensory and swallowing characteristics of high-pressure-heat-treated pork meat gel as a dysphagia diet. Meat Sci. 93(4):843–848.
   PubMed Web of Science ®Google Scholar
• Tsunashima, Y. and Akutagawa, T. (2004). Structure transition in myosin association with the change of concentration: Solubility equilibrium under specified KCl and pH condition. Biopolymers. 75(3):264–277.
   PubMed Web of Science ®Google Scholar
• Undeland, I., Kelleher, S. D. and Hultin, H. O. (2002). Recovery of functional proteins from herring (clupea harengus) light muscle by an acid or alkaline solubilization process.J. Agric. Food Chem. 50(25):7371–7379.
   PubMed Web of Science ®Google Scholar
• Vann, D. G. and Mireles DeWitt, C. A. (2007). Evaluation of solubilized proteins as an alternative to phosphates for meat enhancement. J. Food Sci. 72(1):C072–C077.
   PubMed Web of Science ®Google Scholar
• Wang, Y., Wang, R., Chang, Y., Gao, Y., Li, Z. and Xue, C. (2015). Preparation and thermo-reversible gelling properties of protein isolate from defatted Antarctic krill (euphausia superba) byproducts. Food Chem. 188:170–176.
   PubMed Web of Science ®Google Scholar
• Warriss, P. (2000). Post-mortem changes in muscle and its conversion into meat. Meat Science: An introductory text. 2:93–105.
   Google Scholar
• Weber, G. (1992). Protein Interactions. Chapman and Hall, New York.
   Google Scholar
• Wong, B. T., Day, L. and Augustin, M. A. (2011). Deamidated wheat protein–dextran Maillard conjugates: Effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocolloids. 25(6):1424–1432.
   Web of Science ®Google Scholar
• Xiong, Y. L. (1994). Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing. Crit. Rev. Food Sci. 34(3):293–320.
   PubMed Web of Science ®Google Scholar
• Xiong, Y. L. (2005). Role of myofibrillar proteins in water-binding in brine-enhanced meats. Food Res. Int. 38(3):281–287.
   Web of Science ®Google Scholar
• Xiong, Y. L. and Brekke, C. J. (1991). Protein extractability and thermally induced gelation properties of myofibrils isolated from pre‐and postrigor chicken muscles. J. Food Sci. 56(1):210–215.
   Web of Science ®Google Scholar