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花生蛋白高水分挤压组织化过程中的化学键变化
Changes of Chemical Bonds in Peanut Protein High Moisture Extrusion Texturization
【摘要】 【目的】从挤压产品微观结构、化学键变化和蛋白质酰化改性等方面,探讨花生蛋白高水分挤压组织化结构的形成机理。【方法】采用扫描电子显微镜观察挤压产品的微观结构,利用物性测定仪分析挤压产品的质构特性,用化学分析方法对蛋白质中的总巯基和二硫键含量进行分析,采用琥珀酰化的方法对花生蛋白进行酰化处理。【结果】蛋白质溶解度试验结果显示,随挤压温度的升高,花生蛋白的溶解度迅速降低,在含2%SDS和2%SDS+2%2-ME缓冲液中的溶解度显著增加,最高达76.89%(140℃),说明挤压产品中以非共价键结合的蛋白质含量显著增加。随挤压温度的增加,二硫键含量在140~150℃范围内呈缓慢下降趋势,在155℃时显著降低。花生蛋白质酰化后,挤压产品的硬度、咀嚼度和组织化度等显著降低,相应的微观结构也显示出显著的变化。【结论】在花生蛋白高水分挤压组织化过程中,疏水作用和氢键起主要作用,其次是二硫键。在挤压过程中,花生蛋白分子内原有的二硫键含量降低,可能发生了部分断裂,高温会加速该反应的进行。酰化改性明显干扰了蛋白质分子间的相互作用,不利于挤压产品良好组织化结构的形成。
【Abstract】 【Objective】In this study, the mechanisms of peanut protein high moisture extrusion texturization were explored by analyzing the changes of microstructure, chemical bonds of extrudates and peanut protein succinylated modification before extrusion. 【Method】The microstructures of extrudates were observed by scanning electron microscope. Texture properties of extrudates were analyzed by a texture profile and the chemical methods were used to determine the total sulphhydryl and disulfide bonds contents of extrudates. Peanut protein was modified by succinylation before extrusion. 【Result】The protein solubility test results shows, the solubility of peanut protein was greatly decreased with extrusion temperature increasing, but the protein solubility obviously increased when buffers contained sodium dodecyl sulphate (SDS) alone or in combination with 2-mercaptoethanol (2-ME). The results indicated that the protein which combined by non-covalent bonds increased greatly. The disulphide bond contents of extrudates slightly decreased at 140-150℃, and decreased significantly at 155℃ with the extrusion temperature increasing. When peanut protein was modified by succinylation before extrusion, the hardness, chewiness and texturized index of extrudates were significantly decreased, and the microstructure of corresponding extrudates also present changes.【Conclusion】Hydrophobic interactions and hydrogen bonds played the main function, and disulfide bonds was the second during peanut protein texturization. Some disulfide bonds might be cleaved during extrusion, and the reaction would be accelerated at higher temperatures. Succinylated modification of peanut protein before extrusion could disturb the interactions between protein molecules and hindered the fibrous structure formation during extrusion texturization.
【Key words】 Peanut (Arachis hypogaea L.); Protein; Extrusion texturization; Chemical bonds; Succinylated modification;
- 【文献出处】 中国农业科学 ,Scientia Agricultura Sinica , 编辑部邮箱 ,2007年11期
- 【分类号】S565.2
- 【被引频次】41
- 【下载频次】612