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pH对肌原纤维蛋白二级结构及其热诱导凝胶特性的影响
引用本文: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[J].中国农业科学,2010,43(1):164-170.
作者姓名:费英  韩敏义  杨凌寒  周光宏  徐幸莲  彭增起
作者单位:(南京农业大学食品科技学院/农业部农畜产品加工与质量控制重点开放实验室);
摘    要:【目的】研究pH对猪肉肌原纤维蛋白二级结构α-螺旋及其热诱导凝胶硬度、保水性及微观结构的影响。【方法】采用圆二色谱(circular dichroism,CD)测定不同pH下,猪肉肌原纤维蛋白α-螺旋含量的变化;用物性测试仪测定相应pH下肌原纤维蛋白热诱导凝胶的硬度,用离心法测定其保水性,同时利用扫描电镜拍摄其微观结构。【结果】随着pH偏离肌原纤维蛋白等电点(pI)向中性范围靠近,其α-螺旋含量及其热诱导凝胶的保水性都逐渐增大;而凝胶硬度在pH6.0时达最大值;在远离等电点的中性条件下,肌原纤维蛋白凝胶具有较高有序性的微观结构,而且结构均匀,酸性条件下凝胶的微观结构有序性低,不均匀,且存在聚合物。【结论】猪肉肌原纤维蛋白α-螺旋含量与其热诱导凝胶保水性呈正相关关系;蛋白含天然结构α-螺旋较多时,凝胶微观结构比较有序,反之,凝胶微观结构比较粗糙。

关 键 词:猪肉肌原纤维蛋白  pH  α-螺旋  硬度  保水性  微观结构
收稿时间:2009-05-21;

Studies on the Secondary Structure and Heat-Induced Gelation of Pork Myofibrillar Proteins as Affected by pH
FEI Ying,HAN Min-yi,YANG Ling-han,ZHOU Guang-hong,XU Xing-lian,PENG Zeng-qi.Studies on the Secondary Structure and Heat-Induced Gelation of Pork Myofibrillar Proteins as Affected by pH[J].Scientia Agricultura Sinica,2010,43(1):164-170.
Authors:FEI Ying  HAN Min-yi  YANG Ling-han  ZHOU Guang-hong  XU Xing-lian  PENG Zeng-qi
Affiliation:FEI Ying1,HAN Min-yi1,2,YANG Ling-han1,ZHOU Guang-hong1,XU Xing-lian1,PENG Zeng-qi1 (1Key Laboratory of Meat Processing , Quality Control,Ministry of Education/College of Food Science , Technology,Nanjing Agricultural University,Nanjing 210095,2College of Bioscience , Bioengineering,Hebei University of Science , Technology,Shijiazhuang 050018)
Abstract:Objective]The objective is to study the effect of pH on the secondary structure, α-helix of pork myofibrillar protein, and the hardness, water holding capacity (WHC) and microstructure of its heat-induced gel. Method ] The α-helix of pork myofibrillar protein under different pH were measured by circular dichroism (CD), and the hardness, WHC and microstructure of the heat-induced gel were determined by texture analyzer, centrifugation method and scanning electron microscope (SEM), respectively.Result] The α-helix of pork myofibrillar protein and WHC of its heat-induced gel increased with pH away from pI, the hardness reached its maximum when pH was 6.0, the gel had a uniform and orderly microstructure in neutral, while it had disorderly and uneven microstructure with polymer in the acidic. Conclusion] The α-helix of myofibrillar protein is positive correlated with the WHC of its heat-induced gelation, and the gel has an orderly microstructure with more a-helix, while rough microstructure with less α-helix.
Keywords:pH  pork myofibrillar protein  pH  hardness  water holding capacity  microstructure
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