谷胱甘肽对小麦粉面筋聚集特性的影响

    Effect of glutathione on gluten aggregation properties of wheat flour

    • 摘要: 为了探明还原型谷胱甘肽(GSH)对小麦粉面筋聚集特性的影响及GSH影响面筋聚集特性的分子机制,以郑麦136为试验材料,利用面筋聚集仪研究了小麦粉在还原剂GSH作用下面筋聚集特性的变化,并分析了面筋起始聚集时悬浮液中游离巯基和二硫键含量的变化。结果表明:随着GSH浓度升高,样品中面筋聚集时间缩短,峰值最大时间和面筋聚集能逐渐减小,峰值扭矩无显著变化,最大扭矩120 s后的扭矩减小量逐渐增加;面筋聚集起始点处蛋白质游离巯基含量逐渐增加,二硫键的含量逐渐减小。GSH的存在破坏了面粉中蛋白质间(内)的二硫键,加速了搅拌过程中面粉中蛋白质的解聚分离过程,成为阻止聚合反应的终止剂,阻碍了蛋白质参与面筋的交联,最终导致面筋的聚集特性减弱。

       

      Abstract: This study aimed to evaluate the effects of reduced glutathione(GSH)on the gluten aggregation properties of wheat flour and its molecular mechanism.Zhengmai 136 was used as the experimental material, and the gluten aggregation characteristics of wheat flour in response to reduced glutathione(GSH)were studied using the gluten peak tester.The content of free sulfhydryl groups and disulfide bonds in the suspension when gluten started to aggregate was analyzed.The results showed that with the increase of GSH, the gluten aggregation time decreased, the peak maximum time and gluten aggregation energy decreased gradually, the maximum torque did not change significantly, and the decrease in torque 120 s after maximum torque gradually increased.The content of free sulfhydryl groups at the starting point of gluten aggregation gradually increased and the content of disulfide bonds gradually decreased.Taken together, GSH broke the disulfide bonds of inter/intra proteins in wheat flour, accelerated the depolymerization of proteins, and hindered the participation of proteins in cross-linking of gluten, weakening the aggregation characteristics of gluten.

       

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