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从质构学角度研究肌原纤维蛋白凝胶形成的作用力 被引量:15

Study on Molecular Forces in the Formation in Myofibrillar Protein Gelation from Textural Perspective
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摘要 通过研究有关试剂对肌原纤维蛋白(MP)凝胶质构特性的影响,探讨了维持凝胶形成的作用力。结果表明:改变pH和离子强度影响了静电相互作用,从而改变了肌源纤维蛋白(MP)凝胶的质构特性;添加二硫苏糖醇(DTT)、N-乙基顺丁烯二酰亚胺(NEM)、溴酸钾能影响二硫键的形成,但MP凝胶质构特性变化不明显,说明二硫键对MP凝胶形成的影响不大;添加微量的十二烷基硫酸钠(SDS)可明显影响凝胶的硬度和弹性,说明疏水相互作用在MP凝胶形成中具有显著作用;添加尿素和盐酸胍能明显降低MP凝胶的硬度和弹性,说明氢键对MP凝胶的形成也具有重要的影响。 The molecular forces in the formation of myofibrillar protein gelatin was investigated by determining the effects of the solvents on the textural properties of myofibrillar protein. Ionic strength and pH influenced the electrostatic forces, and changed the textural properties of MP gels. The addition of DTT, NEM and potassium bromate influenced formation of disulfide bond with little changes of textural properties, so the disulfide bond have little effect on the formation of MP gelatin. A few addition of SDS influenced hard- ness and springiness of MP gels obviously. Therefore, the hydrophobic interaction was an important contribution for the formation of MP gelatin. The addition of urea and GuHCl decreased hardness and springiness of MP gels obviously which indicated that hydrogen bonds also had significant effect on the formation of MP gelatin.
出处 《食品与发酵工业》 CAS CSCD 北大核心 2009年第5期45-49,共5页 Food and Fermentation Industries
基金 江苏省自然基金资助项目(KB2006175)
关键词 肌原纤维蛋白 凝胶 质构特性 分子间作用力 myofibrillar protein, gel, texture properties, molecular force
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参考文献15

  • 1王苑,杨玉玲,周光宏,朱学伸.高压预处理及加热方式对混合蛋白凝胶特性的影响[J].食品与发酵工业,2007,33(7):18-21. 被引量:17
  • 2Egelandsdal B. Dynamic rheological measurements on heat-induced myosin gel: Effect of ionic strength , protein concentration and addition of adenosine triphosphate or pyrophosphate[J]. J Sci Food Agric, 1986,37 : 915 - 9 261.
  • 3Niwa E, Matsubara Y, Hamada I. Pariticipation of disulfide bonding in the appearance of setting bull [J].Jap Soc Sci Fish, 1982, 48:727.
  • 4Smyth AB, Smith DM, O' neill E. Disulfide Bonds influence the head induced chicken breast muscle myosin[J]. Food Sci, 1998, 63(4):584.
  • 5WenChing Ko, Chi Cheng Yu, Kuo Chiang Hsu. Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment[J]. Food Science and Technology, 2007,10 : 1 -- 5.
  • 6Sano T, Ohno T, Matsunoi J J, et al. Carp Natural actomyosin., thermal denaturation mechanism[J]. Food Sci, 1994,59:1 002--1 008.
  • 7Hamnda S, Nakai S. Contribution of hydrophobicity, net charge and sulphydryl groups to thermal propertied of ovalbumin[J]. Can Inst Food Sci Technol, 1985,18: 290--295.
  • 8Gill T A, Conway J T. Thermal aggregation of cod muscle proteins using 1 ethyl-3-(3-simethylaminopropyl) carbodimiimide as a zero length cross-linker[J].Agric Boil Chem, 1989,53..2 353.
  • 9杨玉玲,姜攀,贾继荣,马云.鸡肉肌原纤维蛋白与卡拉胶混合凝胶质构特性的研究[J].食品与发酵工业,2008,34(6):16-19. 被引量:18
  • 10郭世良,赵改名,王玉芬,张春晖,郝红涛.离子强度和pH值对肌原纤维蛋白热诱导凝胶特性的影响[J].食品科技,2008,33(1):84-87. 被引量:33

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