物理处理对大豆蛋白-磷脂酰胆碱结构影响的拉曼分析  

Raman Analysis of Influence of Physical Treatment on Structure and Interaction of Soybean Protein-Phosphatidylcholine

作　　者：江连洲[1] 张潇元[1] 朱一方 李杨[1] OLGA Olegovna Babich 王中江[1] 

机构地区：[1]东北农业大学食品学院,哈尔滨150030 [2]克麦罗沃国立大学食品科学与技术学院,克麦罗沃650056

出　　处：《农业机械学报》2018年第2期345-350,共6页Transactions of the Chinese Society for Agricultural Machinery

基　　金：国家自然科学基金面上项目(31671807;31571876);山东省泰山产业领军人才工程高效生态农业创新类项目(LJNY201607);霍英东教育基金会高等院校青年教师基金项目(20152325210002);黑龙江省现代农业产业技术协同创新体系岗位专家项目;黄河三角洲学者岗位项目

摘　　要：利用拉曼光谱技术分析了超声处理及高压均质作用下大豆蛋白-磷脂酰胆碱复合物结构的变化规律。研究表明,超声处理及高压均质处理均提高了大豆蛋白α-螺旋结构及无规则卷曲结构含量,并降低了大豆蛋白的β-构型结构。大豆蛋白-磷脂酰胆碱交互作用显著降低了蛋白质α-螺旋结构,并转变为无规则卷曲结构及β-折叠结构。超声处理及高压均质作用下大豆蛋白-磷脂酰胆碱复合物中蛋白质α-螺旋结构均低于高速分散处理组,而β-折叠结构及无规则卷曲结构含量较高。超声处理、高压均质作用下大豆蛋白色氨酸、酪氨酸残基趋于"暴露态",促进了与磷脂酰胆碱之间的疏水交互作用。大豆蛋白-磷脂酰胆碱的交互作用位点为大豆蛋白疏水氨基酸侧链及磷脂酰胆碱疏水脂链,两者之间的疏水作用是大豆蛋白-磷脂酰胆碱交互作用的主要形式。超声处理、高压均质作用下大豆蛋白二硫键构型未发生显著变化,仍保持旁-旁-反式构象振动模式。大豆蛋白-磷脂酰胆碱交互作用也未改变二硫键构型。Structural changes of soybean protein-phosphatidylcholine complex under ultrasonic treatment and high pressure homogenization by Raman spectroscopy were analyzed. Ultrasonic treatment and high pressure homogenization treatment both were found increased the content of α-helix and random coil structure,but decreased the β-structure of soybean protein. The interaction of soybean protein and phosphatidylcholine significantly decreased the protein α-helix structure by transforming it into random coil and β-sheet structures. Under ultrasonic treatment and high pressure homogenization,the protein α-helix structure of soybean protein-phosphatidylcholine complex was lower than that of the high speed dispersion treatment complex,while the content of β-folded structure and random coil structure were higher. Tryptophan and tyrosine residues of soybean protein tended to expose with ultrasound and high pressure homogenization, which promoted the hydrophobic interaction between soybean protein and phosphatidylcholine. The interaction sites were located in soybean protein hydrophobic amino acid side chain and phosphatidylcholine lipid hydrophobic chain,the hydrophobic interaction was the main force of soybean-phosphatidylcholine interaction. Under the condition of ultrasonic treatment and high pressure homogenization,the structure of disulfide bond of soybean protein was not changed significantly,and the gauche-gauche-trans conformational vibration mode was remained. The interaction of soybean protein phosphatidylcholine did not change the structure of disulfide bond.

关 键 词：大豆蛋白 超声处理 高压均质 拉曼光谱 

分 类 号：TS201.2[轻工技术与工程—食品科学]