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用自旋滴体积法分别测定了大豆分离蛋白和水解度为ＤＨ６．４％的大豆水解蛋白在茴香油／水界面的界面张力。研究表明：两种大豆蛋白质在界面吸附的过程是相似的；大豆分离蛋白的松驰时间τ１与其体相的浓度无关，而大豆水解蛋白的松驰时间τ１与其体相的浓度有关，说明大豆分离蛋白在水溶液中为球蛋白，当它水解到ＤＨ６．４％时，分子呈伸展型柔性分子；大豆水解蛋白的松驰时间τ１和τ２都比大豆分离蛋白小，显然大豆水解蛋白（ＤＨ６．４％）分子扩散到茴香油／水界面的速率以及在界面上分子的重排都比大豆分离蛋白分子快；通过蛋白质的分子量分布的测定，表明大豆水解蛋白分子较小因而扩散较快。
The spinodal volume method was used to determine the interfacial tension between soy protein isolate and soy protein hydrolyzate DH6.4% at the oil / water interface of anise. The results showed that the adsorption process of two kinds of soy protein was similar at the interface; the relaxation time τ1 of soy protein isolate was independent of the concentration of soy protein, while the relaxation time τ1 of soy protein hydrolyzate was related to the concentration of soy protein, The protein is a globulin in aqueous solution. When hydrolyzed to DH6.4%, the molecule is a stretched flexible molecule. The relaxation time τ1 and τ2 of the hydrolyzed protein of soybean are both smaller than that of the soy protein isolate. Apparently, the hydrolyzed protein of soybean (DH6.4 %) Molecules diffused into the oil / water interface of the anise oil, and molecular rearrangement at the interface was faster than those of the soy protein isolate. The determination of the molecular weight distribution of the protein indicated that the molecular weight of the soybean hydrolyzed protein was small and thus diffused rapidly.