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当前位置: 首页 > 文章 > 超声改性大豆亲脂蛋白-羟丙基甲基纤维素乳液的冻融稳定性 食品科学 2020 (5) 73-79
Position: Home > Articles > Freeze-Thaw Stability of Sonicated Soybean Lipophilic Protein-Hydroxypropyl Methylcellulose Stabilized Emulsions FOOD SCIENCE 2020 (5) 73-79

超声改性大豆亲脂蛋白-羟丙基甲基纤维素乳液的冻融稳定性

作  者：
钟明明;廖一;齐宝坤;方琳;孙禹凡;谢凤英;李杨
单  位：
东北农业大学国家大豆工程技术研究中心;东北农业大学食品学院;哈尔滨市食品产业研究院
关键词：
超声;大豆亲脂蛋白;羟丙基甲基纤维素;乳液;冻融稳定性
摘  要：
采用不同超声功率处理的大豆亲脂蛋白(soybean lipoprotein,SLP)与羟丙基甲基纤维素(hydroxypropyl methylcellulose,HPMC)形成复合乳液,通过对其冻融稳定性进行研究,揭示乳液冻融稳定机理与形成乳液复合物结构特性之间的构效关系。结果表明:乳液经两次冻融循环后,随着超声功率的增加,聚结程度降低,400 W超声处理的SLP与HPMC形成的复合乳液最为稳定;经过超声处理的SLP构成的SLP-HPMC复合乳液出油率显著低于未经超声处理的SLP乳液(P<0.05);不同超声功率处理改变了SLP二级结构,400 W超声处理SLP中β-折叠和β-转角的相对含量最大,β-折叠和β-转角的松散结构使蛋白柔性增加,结构更易发生改变和伸展,影响乳液界面复合物的稳定性,进而影响SLP-HPMC复合乳液的冻融稳定性。
译  名：
Freeze-Thaw Stability of Sonicated Soybean Lipophilic Protein-Hydroxypropyl Methylcellulose Stabilized Emulsions
作  者：
ZHONG Mingming;LIAO Yi;QI Baokun;FANG Lin;SUN Yufan;XIE Fengying;LI Yang;School of Food Science, Northeast Agricultural University;Harbin Food Industry Research Institute;National Research Center of Soybean Engineering and Technology, Northeast Agricultural University;
关键词：
ultrasound;;soybean lipophilic protein;;hydroxypropyl methylcellulose;;emulsion;;freeze-thaw stability
摘  要：
In this paper, the freeze-thaw stability of emulsions stabilized by soybean lipophilic protein(SLP) treated with different ultrasonic powers and hydroxypropyl methylcellulose(HPMC) was studied and the underlying mechanism was evaluated from the perspective of structure-activity relationship. The results showed that the degree of aggregation of emulsions subjected to two freeze-thaw cycles was reduced with the increase of ultrasonic power, and the composite emulsion with SLP sonicated at 400 W and HPMC was the most stable. The oil release rate of sonicated SLP-HPMC emulsions was significantly lower than that of unsonicated SLP-HPMC emulsion(P < 0.05). Sonication treatment changed the secondary structure of SLP; the highest contents of β-sheet and β-turn in sonicated SLP were observed at 400 W ultrasonic power, and the loose structures of β-sheet and β-turn contributed to increased protein flexibility and to higher susceptibility to structural changes and unfolding, affecting the interfacial stability and consequently the freeze-thaw stability of the SLP-HPMC composite emulsion.

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