Gelling properties of myofibrillar protein from abalone (Haliotis Discus Hannai Ino) muscle

References

• Anonymous. China Fisheries Yearbook; China Agricultural Press: Beijing, 2016; pp 32–34.
   Google Scholar
• Gao, X.; Tashiro, Y.; Ogawa, H. Rheological Properties and Structural Changes in Raw and Cooked Abalone Meat. Fisheries Science 2001, 67(2), 314–320. DOI: 10.1046/j.1444-2906.2001.00232.x.
   Web of Science ®Google Scholar
• Gao, X.; Tashiro, Y.; Ogawa, H. Rheological Properties and Structural Changes in Steamed and Boiled Abalone Meat. Fisheries Science 2002, 68(3), 499–508. DOI: 10.1046/j.1444-2906.2002.00454.x.
   Web of Science ®Google Scholar
• Gao, X.; Tashiro, Y.; Ogawa, H. The Correlation between Rheological Properties and Characteristic Values of Structure for Steamed Abalone Meat. Food Science and Technology Research 2002, 8(4), 304–310. DOI: 10.3136/fstr.8.304.
   Web of Science ®Google Scholar
• Zhu, B. W.; Dong, X. P.; Sun, L. M.; Xiao, G. H.; Chen, X. J.; Murata, Y.; Yu, C. X. Effect of Thermal Treatment on the Texture and Microstructure of Abalone Muscle (Haliotis Discus). Food Science and Biotechnology 2011, 20(6), 1467–1473. DOI: 10.1007/s10068-011-0203-6.
   Web of Science ®Google Scholar
• Sun, X. D.; Holley, R. A. Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods. Comprehensive Reviews in Food Science and Food Safety 2011, 10(1), 33–51. DOI: 10.1111/crfs.2011.10.issue-1.
   Web of Science ®Google Scholar
• Offer, G.; Trinick, J. On the Mechanism of Water Holding in Meat: The Swelling and Shrinking of Myofibrils. Meat Science 1983, 8(4), 245–281. DOI: 10.1016/0309-1740(83)90013-X.
   PubMed Web of Science ®Google Scholar
• Lin, W. L.; Zeng, Q. X.; Zhu, Z. W.; Song, G. S. Relation between Protein Characteristics and TPA Texture Characteristics of Crisp Grass Carp (Ctenopharyngodon idellus C. Et V) and Grass Carp (Ctenopharyngodon idellus). Journal of Texture Studies 2012, 43(1), 1–11. DOI: 10.1111/j.1745-4603.2011.00311.x.
   Web of Science ®Google Scholar
• Shin, H. G.; Choi, Y. M.; Kim, H. K.; Ryu, Y. C., .; Lee, S. H.; Kim, B. C. Tenderization and Fragmentation of Myofibrillar Proteins in Bovine Longissimus Dorsi Muscle Using Proteolytic Extract from Sarcodon aspratus. LWT-Food Science and Technology 2008, 41(8), 1389–1395. DOI: 10.1016/j.lwt.2007.08.019.
   Web of Science ®Google Scholar
• Lanier, T. C.; Carvajal, P.; Yongsawatdigul, J. Surimi Gelation Chemistry. In Surimi and Surimi Seafood, 2nd ed.; Park, J. W., Ed.; CRC Press: Florida, 2005; pp 436–489.
   Google Scholar
• Dong, X. P.; Ma, L. L.; Zheng, J.; Wang, J. T.; Wu, Q.; Song, S.; Zhou, D. Y. Effect of pH on the Physicochemical and Heat-Induced Gel Properties of Scallop Patinopecten Yessoensis Actomyosin. Fisheries science 2014, 80(5), 1073–1082. DOI: 10.1007/s12562-014-0778-y.
   Web of Science ®Google Scholar
• Liu, R.; Zhao, M. S.; Liu, M. Y.; Yang, H.; Xiong, B. S.; Xie, J. B.; Qin, H. L. Effect of pH on the Gel Properties and Secondary Structure of Fish Myosin. Food Chemistry 2010, 121(1), 196–202. DOI: 10.1016/j.foodchem.2009.12.030.
   Web of Science ®Google Scholar
• Kristinsson, H. G.; Liang, Y. Effect of pH-Shift Processing and Surimi Processing on Atlantic Croaker (Micropogonias undulates) Muscle Proteins. Journal of Food Science 2006, 71(5), C304–C312. DOI: 10.1111/jfds.2006.71.issue-5.
   Web of Science ®Google Scholar
• Dong, X. P.; Li, Y.; Song, L.; Wang, Y.; Tan, M. Q.; Zhu, B. W. Changes of Water Distribution and Physicochemical Properties of Abalone (Haliotis Discus) Myofibrillar Proteins during Heat-Induced Gelation. Journal of Food Processing and Preservation 2016, 41(4).
   Web of Science ®Google Scholar
• Paredi, M. E.; Mattio, N. D. E. V.; Crupkin, M. Biochemical Properties of Actomyosin of Cold Stored Striated Adductor Muscles of Aulacomya Ater Ater (Molina). Journal of Food Science 1990, 55(6), 1567–1570. DOI: 10.1111/j.1365-2621.1990.tb03570.x.
   Web of Science ®Google Scholar
• Lowry, O. H.; Rosebrough, N. J.; Farr, A. L.; Randall, R. J. Protein Measurement with the Folin Henol Reagent. Journal of Biological Chemistry 1951, 193(1), 265–275.
   PubMed Web of Science ®Google Scholar
• Tang, C. H.;. Functional Properties and in Vitro Digestibility of Buckwheat Protein Products: Influence of Processing. Journal of Food Engineering 2007, 82(4), 568–576. DOI: 10.1016/j.jfoodeng.2007.01.029.
   Web of Science ®Google Scholar
• Laemmli, U. K.;. Cleavage of Structural Proteins during Assembly of Head of Bacteriophage T4. Nature 1970, 227(5259), 680–685. DOI: 10.1038/227680a0.
   PubMed Web of Science ®Google Scholar
• Kocher, P. N.; Foegeding, E. A. Microcentrifuge-Based Method for Measuring Water-Holding of Protein Gel. Journal of Food Science 1993, 58(5), 1040–1046. DOI: 10.1111/j.1365-2621.1993.tb06107.x.
   Web of Science ®Google Scholar
• Weng, W. Y.; Zheng, W. X. Silver Carp (Hypophthalmichthys molitrix) Surimi Acid-Induced Gel Extract Characteristics: A Comparison with Heat-Induced Gel. International Journal of Food Properties 2015, 18(4), 821–832. DOI: 10.1080/10942912.2013.864675.
   Web of Science ®Google Scholar
• Ni, N.; Wang, Z.; He, F.; Wang, L.; Pan, H.; Li, X.; Wang, Q. Gel Properties and Molecular Forces of Lamb Myofibrillar Protein during Heat Induction at Different pH Values. Process Biochemistry 2014, 49(4), 631–636. DOI: 10.1016/j.procbio.2014.01.017.
   Web of Science ®Google Scholar
• Lefevre, F.; Fauconneau, B.; Ouali, A.; Culioli, J. Thermal Gelation of Brown Trout Myofibrils from White and Red Muscles: Effect of pH and Ionic Strength. Journal of the Science of Food and Agriculture 2002, 82(4), 452–463. DOI: 10.1002/(ISSN)1097-0010.
   Web of Science ®Google Scholar
• Autio, K.; Kiesvaara, M.; Polvinen, K. Heat-Induced Gelation of Minced Rainbow Trout (Salmo gairdneri): Effect of pH, Sodium Chloride and Setting. Journal of Food Science 1989, 54(4), 805–808. DOI: 10.1111/jfds.1989.54.issue-4.
   Web of Science ®Google Scholar
• Lan, Y. H.; Novakofski, J.; McCusker, R. H.; Brewer, M. S.; Carr, T. R.; McKeith, F. K. Thermal Gelation of Myofibrils from Pork, Beef, Fish, Chicken and Turkey. Journal of food science 1995, 60(5), 941–945. DOI: 10.1111/jfds.1995.60.issue-5.
   Web of Science ®Google Scholar
• Ehara, T.; Nakagawa, K.; Tamiya, T.; Noguchi, S. F.; Tsuchiya, T. Effect of Paramyosin on Invertebrate Natural Actomyosin Gel Formation. Fisheris Science 2004, 70(2), 306–313. DOI: 10.1111/j.1444-2906.2003.00805.x.
   Web of Science ®Google Scholar
• Liu, R.; Zhao, M. S.; Xiong, B. S.; Xie, J. B.; Qin, H. L. Role of Secondary Structures in the Gelation of Porcine Myosin at Different pH Values. Meat Science 2008, 80(3), 632–639. DOI: 10.1016/j.meatsci.2008.02.014.
   PubMed Web of Science ®Google Scholar
• Chung, Y. C.; Richardson, L.; Morrissey, M. T. Effects of pH and NaCl on Gel Strength of Pacific Whiting Surimi. Journal of Aquatic Food Product Technology 1994, 2(3), 19–35. DOI: 10.1300/J030v02n03_03.
   Google Scholar
• Paredi, M. E.; Tomas, M. C.; Crupkin, M. Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study. Journal of Agricultural and Food Chemistry 2002, 50(4), 830–834. DOI: 10.1021/jf010767q.
   PubMed Web of Science ®Google Scholar
• Mizuno, A.; Mitsuiki, M.; Motoki, M.; Ebisawa, K.; Suzuki, E. I. Relationship between the Glass Transition of Soy Protein and Molecular Structure. Journal of Agricultural and Food Chemistry 2000, 48(8), 3292–3297. DOI: 10.1021/jf991151s.
   PubMed Web of Science ®Google Scholar
• Sun, X. D.; Arntfield, S. D. Molecular Forces Involved in Heat-Induced Pea Protein Gelation: Effects of Various Reagents on the Rheological Properties of Salt-Extracted Pea Protein Gels. Food Hydrocolloid 2012, 28(2), 325–332. DOI: 10.1016/j.foodhyd.2011.12.014.
   Web of Science ®Google Scholar
• Taylor, L. S.; Zografi, G. Sugar–Polymer Hydrogen Bond Interactions in Lyophilized Amorphous Mixtures. Journal of pharmaceutical sciences 1998, 87(12), 1615–1621. DOI: 10.1021/js9800174.
   PubMed Web of Science ®Google Scholar
• Larsson, K.; Rand, R. P. Detection of Changes in the Environment of Hydrocarbon Chains by Raman Spectroscopy and Its Application to Lipid-Protein Systems. Biochimica et Biophysica Acta (BBA)-Lipids and Lipid Metabolism 1973, 326(2), 245–255. DOI: 10.1016/0005-2760(73)90250-6.
   PubMed Web of Science ®Google Scholar
• Tolano-Villaverde, I. J.; Ezquerra-Brauer, J. M.; Ocano-Higuera, V. M.; Torres-Arreola, W.; Ramirez-Wong, B.; Herrera-Urbina, R.; Marquez-Rios, E. Effect of pH and Chitosan Concentration on Gelation of Protein Concentrate from Giant Squid Mantle (Dosidicus gigas). International Journal of Food Science and Technology 2016, 51(6), 1360–1368. DOI: 10.1111/ijfs.13095.
   Web of Science ®Google Scholar
• Karthikeyan, S.; Mani, P. Effect of Heavy Metals on Tissue Protein of an Edible Fish Cirrhinus mrigala as Dependent on pH and Water Hardness. Biophysics 2014, 59(2), 321–325. DOI: 10.1134/S0006350914020110.
   Google Scholar
• Pelton, J. T.; McLean, L. R. Spectroscopic Methods for Analysis of Protein Secondary Structure. Analytical Biochemistry 2000, 277(2), 167–176. DOI: 10.1006/abio.1999.4320.
   PubMed Web of Science ®Google Scholar