Scientia Agricultura Sinica ›› 2014, Vol. 47 ›› Issue (10): 2013-2020.doi: 10.3864/j.issn.0578-1752.2014.10.015
• STORAGE·FRESH-KEEPING·PROCESSING • Previous Articles Next Articles
YANG Yu-Ling, YOU Yuan, PENG Xiao-Bei, CHEN Yin-Ji
[1]Sano T, Noguchi S F, Tsuchiya T, Matsumoto J J. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. Journal of Food Science, 1988, 53(3): 924-928.[2]Liu R, Zhao S M, Liu Y M, Yang H, Xiong S B, Xie B J, Qin L H. Effect of pH on the gel properties and secondary structure of fish myosin. Food Chemistry, 2010, 121(1): 196-202.[3]Xu X L, Han M Y, Fei Y, Zhou G H. Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic. Meat Science, 2011, 87(3): 159-164.[4]孔保华, 王宇, 夏秀芳, 刘骞, 李明清. 加热温度对猪肉肌原纤维蛋白凝胶特性的影响. 食品科学, 2011, 32 (05) : 50-54.Kong B H, Wang Y, Xia X F, Liu Q, Li M Q. Influence of heating temperature on gel properties of porcine myofibrillar protein. Food Science, 2011, 32(05): 50-54. (in Chinese)[5]Wang C H, Damodaran S. Thermal gelation of globular proteins: influence of protein conformation on gel strength. Journal of Agricultural and Food Chemistry, 1991, 39(3): 433-438.[6]Xiong Y L, Blanchard S P. Myofibrillar protein gelation: viscoelastic changes related to heating procedures. Journal of Food Science, 1994, 59(4): 734-738.[7]Xiong Y L, Blanchard S P. Dynamic gelling properties of myofibrillar protein from skeletal muscles of different chicken parts. Journal of Agricultural and Food Chemistry, 1994, 42(3): 670-674.[8]Visessanguan W, Ogawa M, Nakai S, An H. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. Journal of Food Science, 2000, 48(4): 1016-1023.[9]Liu W H, Stevenson C D, Lanier T C. Rapid heating of alaska pollock and chicken breast myofibrillar proteins as affecting gel rheological properties. Journal of Food Science, 2013, 78(7): 971-977.[10]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.[11]Gornal A G, Bardawill C J, David M. Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry, 1949, 177(2): 751-766.[12]Whitmore L, Wallace B A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Research, 2004, 32(Web Server Issue): W668-W673.[13]Andrade M A, Chacón P, Merelo J J, Morán F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Engineering Design and Selection, 1993, 6(4): 383-390.[14]费英, 韩敏义, 杨凌寒, 周光宏, 徐幸莲, 彭增起. pH对肌原纤维蛋白二级结构及其热诱导凝胶特性的影响.中国农业科学, 2010, 43(1): 164-170.Fei Y, Han M Y, Yang L H, Zhou G H, Xu X L, Peng Z Q. Studies on the secondary structure and heat-induced gelation of pork myofibrillar proteins as affected by pH. Scientia Agricultura Sinica, 2010, 43(1): 164-170. (in Chinese)[15]Carr H Y, Purcell E M. Effects of diffusion on free precession in nuclear magnetic resonance experiments. Physical Review, 1954, 94(3): 630-638.[16]Meiboom S, Gill D. Modified spin-echo method for measuring nuclear relaxation times. Review of Scientific Instruments, 1958, 29(8): 688-691.[17]Trout G R. Techniques for measuring water-binding capacity in muscle foods—A review of methodology. Meat Science, 1988, 23(4): 235-252.[18]韩敏义, 费英, 徐幸莲, 周光宏. 低场NMR研究pH对肌原纤维蛋白热诱导凝胶的影响. 中国农业科学, 2009, 42(6): 2098-2104.Han M Y, Fei Y, Xu X L, Zhou G H. Heat-induced gelation of myofibrillar proteins as affected by pH—a low field NMR study. Scientia Agricultura Sinica, 2009, 42(6): 2098-2104. (in Chinese)[19]Greenfield N J. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Analytical Biochemistry, 1996, 235(1): 1-10.[20]Yongsawatdigul J, Park J W. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry, 2003, 83(3): 409-416.[21]Hemung B O, Eunice C Y, Chan L, Yongsawatdigul J. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. Food Chemistry, 2008, 111(2): 439-446. [22]Wang H H, Pato M, Pietrasik Z, Shand P. Biochemical and physicochemical properties of thermally treated natural actomyosin extracted from normal and PSE pork Longissimus muscle. Food Chemistry, 2009, 113(1): 21-27.[23]Liu R, Zhao S M, Xiong S B, Xie B J, Qin L H. Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science, 2008, 80(3): 632-639.[24]Westphalen A, Briggs J, Lonergan S M. Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation. Meat Science, 2006, 72(4): 697-703.[25]Westphalen A, Briggs J, Lonergan S M. Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation. Meat Science, 2005, 70(2): 293-299.[26]Kang Z L, Wang P, Xu X L, Zhu C Z, Zou Y F, Li K, Zhou G H. Effect of a beating process, as a means of reducing salt content in Chinese-style meatballs (kung-wan): A dynamic rheological and Raman spectroscopy study. Meat Science, 2014, 96(2): 669-674.[27]Sun X D, Arntfield S D. Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking. Journal of Food Engineering, 2011, 107(2): 226-233.[28]Ogawa M, Kanamaru J, Miyashita H, Tamiya T, Tsuchiya T. Alpha-helical structure of fish actomyosin: changes during setting. Journal of Food Science, 1995, 60(2): 297-299.[29]Fennema O R. Food Chemistry, 3rd Edition. New York: Marcel Dekker, Inc. 1996: 365-393. |
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