Adsorption and Dilatational Rheology of Heat-Treated Soy Protein at the Oil-Water Interface: Relationship to Structural Properties

文献类型： 外文期刊

第一作者： Wang, Jin-Mei

作者： Wang, Jin-Mei;Xia, Ning;Yang, Xiao-Quan;Yin, Shou-Wei;Qi, Jun-Ru;He, Xiu-Ting;Wang, Li-Juan;Xia, Ning;Yuan, De-Bao;Wang, Li-Juan

作者机构：

关键词： soy protein;heat treatment;structural properties;oil-water interface;adsorption;surface dilatational rheology

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： 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 °C). Heat treatment at 90 °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 °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.

分类号： R15

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