热处理对大豆11S球蛋白表面疏水性的影响及拉曼光谱分析  

Effect of Heat Treatment on Surface Hydrophobicity of 11S Glycinin and Raman Spectroscopy Analysis

作　　者：齐宝坤[1] 赵城彬[2] 江连洲[1] 徐靓[1] 李红[1] 李杨[1] QI Baokun;ZHAO Chengbin;JIANG Lianzhou;XU Liang;LI Hong;LI Yang(College of Food Science,Northeast Agricultural University,Harbin 150030,China;College of Food Science and Engineering,Jilin Agricultural University,Changchun 130118,China)

机构地区：[1]东北农业大学食品学院,黑龙江哈尔滨150030 [2]吉林农业大学食品科学与工程学院,吉林长春130118

出　　处：《食品科学》2018年第18期15-20,共6页Food Science

基　　金："十三五"国家重点研发计划重点专项(2016YFD0401402)

摘　　要：研究热处理对大豆11S球蛋白表面疏水性(H_0)的影响,并对蛋白质拉曼光谱进行分析。随着热处理时间的延长,在80℃热处理下,大豆11S球蛋白的H_0增加,二级结构中α-螺旋结构转变为β-转角和无规卷曲结构。在90℃和100℃热处理下,H0先增加后稍有降低,且100℃热处理下H_0变化地更快,且变化程度更大,α-螺旋和β-折叠结构转变为β-转角和无规卷曲结构。此外,热处理会使蛋白分子中的酪氨酸和色氨酸残基趋于"暴露"态,同时改变11S球蛋白分子间二硫键的振动模式,使二硫键由g-g-g构型转变为t-g-t构型,这可能会导致蛋白质H_0的升高。The effect of heat treatment on the surface hydrophobicity(H0)of 11S glycinin was researched and its secondary structure was analyzed by Raman spectroscopy before and after heat treatment.As the heat treatment time increased(80℃),H0 was increased andα-helix was transformed toβ-turn and random coil structures.At both 90 and 100℃,H0 increased first and then decreased,while it changed faster and more significantly at 100℃,andα-helix andβ-sheet were transformed toβ-turn and random coil structures.Moreover,the tyrosine and tryptophan residues in the protein molecule were exposed after heat treatment.At the same time,the vibration mode of intermolecular disulfide bond in 11S glycinin was changed,transforming the disulfide bond from g-g-g configuration to t-g-t configuration,which may lead to an increase in protein surface hydrophobicity.

关 键 词：热处理 大豆11S球蛋白 表面疏水性 拉曼光谱 

分 类 号：TS201.2[轻工技术与工程—食品科学]