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Solubilisation of muscle proteins from chicken breast muscle by ultrasonic radiations in physiological ionic medium

机译:在生理离子介质中通过超声波辐照从鸡胸肌中溶解肌肉蛋白

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Solubilisation of myofibrillar proteins in physiological or low ionic strength solutions is essential for their utilisation as supplementary protein food. In order to achieve low ionic strength solubility, ultrasonication as a physical force has been introduced as an effective method to shift the solubility range of myofibrillar proteins from high to low ionic medium. In this study, change in the solubility behaviour of extracted actomyosin by ultrasonication in tris-maleate (with/without 0.1?M NaCl) and water is studied. Our results demonstrate that ultrasonication solubilises actomyosin in all the three investigated systems i.e. tris-maleate (with 0.1?M NaCl), tris-maleate only (without 0.1?M NaCl) and water. A decreasing trend in the investigated biochemical parameters such as ATPases (Ca~(2+), Mg~(2+)) and turbidity was observed as a result of ultrasonic exposure. Analysis of SDS-PAGE profiles showed least solubility of myosin heavy chain in water compared to tris-maleate (with/without 0.1?M NaCl), while results of electron micrographs reveal change in the degree of dissociation or disruption of actomyosin aggregates according to the time of sonication and the suspension-media type. In conclusion, the results of our study suggest that ultrasonication plays a significant role in solubilisation of major myofibrillar proteins most probably by altering the conformation of actomyosin complex.
机译:肌原纤维蛋白在生理或低离子强度溶液中的增溶对于它们用作补充蛋白食品至关重要。为了获得低离子强度的溶解度,已引入超声作为物理力作为将肌原纤维蛋白的溶解度范围从高离子介质转变为低离子介质的有效方法。在这项研究中,研究了超声作用下提取的肌动球蛋白在马来酸三甲酯(有/无0.1?M NaCl)和水中的溶解行为的变化。我们的结果表明,超声处理能在所有三个研究系统中溶解肌动球蛋白,即马来酸三甲酯(含0.1?M NaCl),马来酸三甲酯(不含0.1?M NaCl)和水。超声暴露结果表明,所研究的生化参数如ATPases(Ca〜(2 +),Mg〜(2+))和浊度呈下降趋势。 SDS-PAGE图谱分析显示,肌球蛋白重链在水中的溶解度比三马来酸酯(有/无0.1?M NaCl)要小,而电子显微照片的结果则表明,根据肌钙蛋白,肌动球蛋白聚集体的解离或破坏程度发生了变化。超声处理的时间和悬浮介质的类型。总之,我们的研究结果表明,超声作用最可能通过改变放线菌素复合物的构象在主要肌原纤维蛋白的增溶中发挥重要作用。

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