Adsorption and Dilatational Rheology of Heat-Treated Soy Protein at the Oil-Water Interface: Relationship to Structural Properties
Adsorption and Dilatational Rheology of Heat-Treated Soy Protein at the Oil-Water Interface: Relationship to Structural Properties
复制标题
热处理大豆蛋白在油水界面的吸附和膨胀流变学：与结构特性的关系
DOI：
10.1021/jf205128v
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发表时间：
2012-03-28
影响因子：
6.1
通讯作者：
Wang, Li-Juan
中科院分区：
文献类型：
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作者：
Wang, Jin-Mei;Xia, Ning;Wang, Li-Juan
我们评估了热处理对大豆分离蛋白的界面性质（在油-水界面的吸附和界面层的流变学）的影响。蛋白质的相关结构特性影响这些界面行为，包括蛋白质的解折叠和聚集，表面疏水性，和巯基的状态，也进行了研究。大豆蛋白的结构和界面性质强烈依赖于加热温度（90和120摄氏度）。在90 ° C下的热处理诱导的表面疏水性增加，由于部分解折叠的蛋白质，伴随着形成的聚集体连接的二硫键，并在长期吸附和类似的动态界面流变学的表面压力较低，观察到相比，天然蛋白质。相比之下，在120摄氏度的热处理导致更高的表面活性的蛋白质和吸附层中的分子间相互作用的快速发展，如表面压力和结晶模量的更快的增加所证明的。这种加热蛋白质的界面行为可能主要与更灵活的构象和高游离巯基有关，即使一些暴露的疏水基团参与形成聚集体。这些结果将有助于更好地理解蛋白质界面行为的结构依赖性，并扩大热处理蛋白质在乳液配制和生产中的利用。
We evaluated the influence of heat treatment on interfacial properties (adsorption at the oil water interface and dilatational rheology of interfacial layers) of soy protein isolate. The related structural properties of protein affecting these interfacial behaviors, including protein unfolding and aggregation, surface hydrophobicity, and the state of sulfhydryl group, were also investigated. The structural and interfacial properties of soy protein depended strongly on heating temperature (90 and 120 degrees C). Heat treatment at 90 degrees C induced an increase in surface hydrophobicity due to partial unfolding of protein, accompanied by the formation of aggregates linked by disulfide bond, and lower surface pressure at long-term adsorption and similar dynamic interfacial rheology were observed as compared to native protein. Contrastingly, heat treatment at 120 degrees C led to a higher surface activity of the protein and rapid development of intermolecular interactions in the adsorbed layer, as evidenced by a faster increase of surface pressure and dilatational modulus. The interfacial behaviors of this heated protein may be mainly associated with more flexible conformation and high free sulfhydryl group, even if some exposed hydrophobic groups are involved in the formation of aggregates. These results would be useful to better understand the structure dependence of protein interfacial behaviors and to expand utilization of heat-treated protein in the formulation and production of emulsions.