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肌球蛋白与胶原蛋白和明胶混合凝胶质构特性的研究 被引量:2

Study on Textural Properties of Myosin-Collagenous Protein and Myosin-Gelatin Mixed Gels
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摘要 研究了肌球蛋白与胶原蛋白、肌球蛋白和明胶混合凝胶的质构特性和保水性。结果表明:肌球蛋白与胶原蛋白、肌球蛋白与明胶混合凝胶的硬度、弹性和保水性均比纯肌球蛋白高。肌球蛋白与胶原蛋白混合凝胶在pH6.0时,硬度最低、保水性最低,但弹性最大。混合凝胶的硬度和保水性随着离子强度的升高而升高,但弹性则恰好相反。添加KCl能显著改善混合凝胶的弹性,添加SPP和TPP能明显提高保水性。肌球蛋白和明胶混合凝胶在pH6.5时硬度和弹性最大,但保水性在pH6.0时最大;其硬度和弹性随离子强度增加而降低,但其保水性刚好相反。 Textural properties and water holding capacities (WHC) of myosin - coUagenous protein and myosin -gelatin mixed gels were studied. The results showed that the values of the hardness, springiness and WHC of myosin - collagenous protein and myosin - gelatin mixed gels were higher than those of pure myosin. The values of the hardness and WHC of myosin - coUagenous protein mixed gel were lowest at pH6.5, whilst the value of the springiness was highest. The hardness and WHC of the myosin - collagenous protein mixed gel increased with the ionic strength, whilst the springiness was the opposite. The springiness of myosin - collagenous protein mixed gel could be improved by adding KCl, and the WHC could be improved by adding SPP and TPP. The values of hardness and springiness of myosin - gelatin mixed gel were highest at pH6.5, whilst the value of the WHC was highest at pH6.0. The hardness and springiness of the myosin - gelatin mixed gel increased with the decrease of ionic strength, but the WHC was the opposite.
出处 《食品科学》 EI CAS CSCD 北大核心 2007年第9期111-116,共6页 Food Science
基金 中国博士后基金资助项目(2005037738) 江苏省博士后基金资助项目 江苏省自然科学基金资助项目(KB2006175)
关键词 肌球蛋白 胶原蛋白 明胶 质构特性保水性 myosin collagenous protein gelatin textural properties water holding capacity
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参考文献6

  • 1EGELANDSDA I B, FRETHEIM K, HARBIZI O. Dynamic rheological measurements on head-induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate[J]. J Sci Food Agric, 1986, 37: 915-926.
  • 2ISHIOROSHI M, SAMEJIIMA K, YASUI T. Heat-induced gelation of myosin: Factors of pH and salt concentration[J]. J Food Sci, 1979, 44: 1280-1286.
  • 3LIU M N, FOEGEDING E A. Thermally induced gelation of chicken myosin isoforms[J]. J Agric Food Chem, 1996, 44: 1441-1446.
  • 4VUORIO E, CROMBRUGGHE B, The family of collagen genes[J]. Annu Review Biochemistry, 1990, 50: 837.
  • 5江晃荣.胶原蛋白的惊人疗效[M].台湾:台湾世茂出版集团,2002.150-190.
  • 6NAUSS K M, KITAGAWA S, GERGELY J. Pyrophosphate binding to and adenosinc triphosphate activity of myosin and its proteolytic fragments [J]. J Biol Chem, 1969, 244(3): 755-765.

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  • 5Li R, Carpenter JA, Cheney R. Sensory and instrumental properties of smoked sausage made with mechanically separated poultry(MSP) meat and wheat protein [ J ]. Journal of Food Sence, 1998,63 ( 5 ) :923- 925.
  • 6Guardia MD, Guerrero L, C, elabert G, et al. Sensory charac- terization and consumer acceptability of small calibre fermen- ted sausages with 50% substitution of NaCI by mixtures of KC1 and potassium lactate [ J ]. Meat Science, 2008,80 : 1225 - 1230.
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  • 8Damodaran S, Paraf A. Food proteins and their application [ M]. New York: Marcel Dekker Ine, 1997:257 - 290.
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  • 10Hoseney RC, Smewing J. Instrumental measurement of stick- iness of doughs and other foods [ J ]. Journal of Texture Stud- ies, 1999,30:123-136.

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