Gelation of salted myofibrillar protein under malondialdehyde-induced oxidative stress
Gelation of salted myofibrillar protein under malondialdehyde-induced oxidative stress
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DOI：
10.1016/j.foodhyd.2014.03.001
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发表时间：
2014-10
影响因子：
10.7
通讯作者：
Feibai Zhou;Mouming Zhao;G. Su;Chun Cui;Weizheng Sun
中科院分区：
文献类型：
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作者：
Feibai Zhou;Mouming Zhao;G. Su;Chun Cui;Weizheng Sun
本研究提出了在0.6 M NaCl存在下，在氧化应激下，由丙二醛（MDA）产生的冷定型肌原纤维蛋白凝胶的形成。还应用加热程序以进一步评价凝胶性质。蛋白质羰基含量用于评价蛋白质氧化。进行十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）以解释凝胶的形成。采用凝胶强度、持水力、扫描电子显微镜（SEM）和傅里叶变换红外光谱（FTIR）等测试方法，比较了不同MDA/NaCl浓度下的凝胶性能。结果证实了所用系统中发生蛋白质氧化。肌球蛋白通过非二硫键共价键参与凝胶形成。同时，随着MDA/NaCl添加量的增加，凝胶强度、持水力、高度多孔的网络结构和形状清晰的网络结构都得到了显著的改善。此外，当MDA的添加量不超过10 mM时，在0.6 M NaCl存在下形成的凝胶对热处理是稳定的，而较高的MDA会导致凝胶塌陷，这被认为是由于存在过量的共价键。在这项研究中的凝胶化过程涉及同时蛋白质氧化和内部交联。该凝胶的形成是以肌原纤维蛋白在一定离子强度下发生溶胀和通过MDA形成的分子间交联为前提的。
This study presented the formation of cold-set myofibrillar protein gel under oxidative stress originated from malondialdehyde (MDA) in the presence of 0.6 M NaCl. Heating procedure was also applied for further evaluation of gel properties. Protein carbonyl content was used to evaluate protein oxidation. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed to explain the formation of the gel. Gel properties were compared in range of MDA/NaCl concentration with use of gel strength, water-holding capacity (WHC), scanning electron microscopy (SEM) and Fourier transform infrared spectroscopy (FTIR) measurements. Results confirmed the occurrence of protein oxidation in the system applied. Myosin was greatly involved in gel formation through non-disulfide covalent bond. Meanwhile, significant improvements in gel strength, WHC, the network structure of highly porous with well-defined shapes were observed with increasing addition of MDA/NaCl. Furthermore, with the addition of MDA no more than 10 mM, the gel formed in the presence of 0.6 M NaCl was stable to heat treatment, while the higher MDA could cause gel collapse, which was believed to be due to the excessive covalent bond existed. The gelation procedure in this study involved simultaneous protein oxidation and internal cross-linking. The gel was formed on the premise of the swelling of myofibrillar protein under certain ionic strength and the intermolecular cross-links formed via MDA.