References
- Aliño, M., Grau, R., Fuentes, A., & Barat, J. M. (2010). Influence of low sodium mixtures of salts on the post-salting stage of dry-cured ham progress. Journal of Food Engineering, 99, 198–205.
- Chen, J., Dickinson, E., & Edwards, M. (1999). Rheology of acid-induced sodium caseinate stabilized emulsion gels. Journal of Texture Studies, 30, 377–396.
- Cheret, R., Chapleau, N., Delbarre-Ladrat., C., Verrez-Bagnis, V., & Lamballerie, M. D. (2005). Effects of high pressure on texture and microstructure of sea bass (Dicentrarchus labrax L.) fillets. Journal of Food Science, 70, E477–E483.
- Fretheim, K., Egelandsdal, B., Harbitz, O., & Samejima, K. (1985). Slow lowering of pH induces gel formation of myosin. Food Chemistry, 18, 169–178.
- Fu, X., Hayat, K., Li, Z., Lin, Q., Xu, S., & Wang, S. (2012). Effect of microwave heating on the low-salt gel from silver carp (Hypophthalmichthys molitrix) surimi. Food Hydrocolloids, 27, 301–308.
- Gargaud, M., Amils, R., Cleaves, H. J., Viso, M., & Pinti, D. (Eds.). (2011). Encyclopedia of astrobiology (Vol. 1). Germany: Springer.
- Goto, Y., Takahashi, N., & Fink, A. L. (1990). Mechanism of acid-induced folding of proteins. Biochemical, 29, 3480–3488.
- Gou, P., Guerrero, L., Gelabert, J., & Arnau, J. (1996). Potassium chloride, potassium lactate and glycine as sodium chloride substitutes in fermented sausages and in dry-cured pork loin. Meat Science, 42, 37–48.
- Greenfield, N. J. (1999). Applications of circular dichroism in protein and peptide analysis. Trac-Trends Analytical Chemistry, 18, 236–244.
- Guàrdia, M. D., Guerrero, L., Gelabert, J., Gou, P., & Arnau, J. (2008). Sensory characterisation and consumer acceptability of small caliber fermented sausages with 50% substitution of NaCl by mixtures of KCl and potassium lactate. Meat Science, 80, 1225–1230.
- Hayakawa, T., Ito, T., & Wakamatsu, J. (2009). Myosin is solubilized in a neutral and low ionic strength solution containing l-histidine. Meat Science, 82, 151–154.
- Hayakawa, T., Yoshida, Y., & Yasui, M. (2012). Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine. Meat Science, 90, 77–80.
- Ishioroshi, M., Jima, K. S., & Yasui, T. (2010). Heat-induced gelation of myosin: Factors of pH and salt concentrations. Journal of Food Science, 44, 1280–1284.
- Kim, B. Y., Park, J. W., & Yoon, W. B. (2005). Rheology and texture properties of surimi gels. In J. W. Park (Ed.), Surimi and surimi seafood (2nd ed., pp. 491–582). New York: Marcel Dekker.
- Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680–685.
- Laniner, T. C., Carvajal, P., & Yongsawatdigul, J. (2005). Surimi gelation chemistry. In J. W. Park (Ed.), Surimi and surimi seafood (2nd ed., pp. 435–477). New York: Marcel Dekker.
- Lin, T. M., & Park, J. W. (2010). Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. Journal of Food Science, 63, 215–218.
- 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.
- Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265–275.
- Martínez, M. A., Robledo, V., Velazquez, G., Ramírez, J. A., Vázquez, M., & Uresti, R. M. (2014). Effect of precooking temperature and microbial transglutaminase on the gelling properties of blue crab (Callinectes sapidus) proteins. Food Hydrocolloids, 35, 264–269.
- Martone, C. B., Busconi, L., Folco, E. J., Trucco, R. E., & Sanchez, J. J. (1986). A simplified myosin preparation from marine fish species. Journal of Food Science, 51, 1554–1555.
- Nayak, R., Kenney, P. B., Slider, S., Head, M. K., & Killefer, J. (1998a). Cook yield, texture and gel ultrastructure of model beef batters as affected by low levels of calcium, magnesium and zinc chloride. Journal of Food Science, 63, 945–950.
- Nayak, R., Kenney, P. B., Slider, S., Head, M. K., & Killefer, J. (1998b). Myofibrillar protein solubility of model beef batters as affected by low levels of calcium, magnesium and zinc chloride. Journal of Food Science, 63, 951–954.
- Privalov, P. L. (1982). Stability of proteins. Proteins which do not present a single cooperative system. Advance in Protein Chemistry, 35, 1–104.
- Regenstein, J. M. (1984). Food protein chemistry (pp. 353). New York: Academic Press.
- Satoh, Y., Nakaya, M., Ochiai, Y., & Watabe, S. (2006). Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack. Fisheries Science, 72, 646–655.
- Steffansson, G., & Hultin, H. O. (1994). On the solubility of cod muscle proteins in water. Journal of Agricultural and Food Chemistry, 42, 2656–2664.
- Suzuki, T. (1981). Fish and krill proteins: processing technology (p. In 260). London, UK: Applied Science Publishing.
- Tahergorabi, R., Beamer, S. K., Matak, K. E., & Jaczynski, J. (2012b). Salt substitution in surimi seafood and its effects on instrumental quality attributes. LWT-Food Science and Technology, 48, 175–181.
- Tahergorabi, R., & Jaczynski, J. (2012a). Physicochemical changes in surimi with salt substitute. Food Chemistry, 132, 1281–1286.
- Xiong, Y. L., & Brekke, C. J. (1991). Gelation properties of chicken myofibrils treated with calcium and magnesium chlorides. Journal of Muscle Foods, 2, 21–36.
- Zhang, Y., Cheng, Q., Yao, Y., Guo, X., Wang, R., & Peng, Z. (2014). A preliminary study: Saltiness and sodium content of aqueous extracts from plants and marine animal shell. European Food Research and Technology, 238, 565–571.
- Zhang, Y., Wu, J., Jamali, M. A., Guo, X., & Peng, Z. (2017). Heat-induced gel properties of porcine myosin in a sodium chloride solution containing l -lysine and l-histidine. LWT - Food Science and Technology, 85. doi:10.1016/j.lwt.2017.06.059
- Zhang, Y. W., Zhang, L., Hui, T., Guo, X. Y., & Peng, Z. Q. (2015). Influence of partial replacement of NaCl by KCl, L-histidine and L-lysine on the lipase activity and lipid oxidation in dry-cured loin process. LWT-Food Science and Technology, 64, 966–973.
- Zhang, Z., Liao, H., Li, H., Nie, L., & Yao, S. (2005). Stereoselective histidine sensor based on molecularly imprinted sol-gel films. Analytical Biochemistry, 336, 108–116.