食品科学 ›› 2020, Vol. 41 ›› Issue (5): 73-79.doi: 10.7506/spkx1002-6630-20190130-390

• 食品工程 • 上一篇    下一篇

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

钟明明,廖一,齐宝坤,方琳,孙禹凡,谢凤英,李杨,   

  1. (1.东北农业大学食品学院,黑龙江 哈尔滨 150030;2.哈尔滨市食品产业研究院,黑龙江 哈尔滨 150000;3.东北农业大学 国家大豆工程技术研究中心,黑龙江 哈尔滨 150000)
  • 出版日期:2020-03-15 发布日期:2020-03-23
  • 基金资助:
    中国博士后科学基金面上项目(2018M631902)

Freeze-Thaw Stability of Sonicated Soybean Lipophilic Protein-Hydroxypropyl Methylcellulose Stabilized Emulsions

ZHONG Mingming, LIAO Yi, QI Baokun, FANG Lin, SUN Yufan, XIE Fengying, LI Yang,   

  1. (1. School of Food Science, Northeast Agricultural University, Harbin 150030, China; 2. Harbin Food Industry Research Institute, Harbin 150000, China; 3. National Research Center of Soybean Engineering and Technology, Northeast Agricultural University, Harbin 150000, China)
  • Online:2020-03-15 Published:2020-03-23

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。

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

Abstract: 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.

Key words: ultrasound, soybean lipophilic protein, hydroxypropyl methylcellulose, emulsion, freeze-thaw stability

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