大豆蛋白-酪蛋白复合物结构的红外光谱分析  

FTIR Analysis on the Structure of Soybean-Casein Protein Complex

作　　者：石彦国[1] 郭庆启[2] 杨晓婉 刘晓飞[1] 王世杰 朱宏 张娜[1] Shi Yanguo;Guo Qingqi;Yang Xiaowan;Liu Xiaofei;Wang Shijie;Zhu Hong;Zhang Na(College of Food Science and Engineering,Harbin University of Commerce,Key Laboratory of Food Science and Engineering of Heilongjiang Province,Harbin 150076;School of Forestry,Northeast Forestry University,Harbin 150040;College of Biological Science and Engineering,Hebei University of Science and Technology,Shijiazhuang 050000;Shijiazhuang Junlebao Dairy Co.LTD,Shijiazhuang 050221)

机构地区：[1]哈尔滨商业大学食品工程学院,黑龙江省食品科学与工程重点实验室,哈尔滨150076 [2]东北林业大学林学院,哈尔滨150040 [3]河北科技大学生物科学与工程学院,石家庄050000 [4]石家庄君乐宝乳业有限公司,石家庄050221

出　　处：《中国食品学报》2018年第11期225-231,共7页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家自然科学基金面上项目(31871747);国家自然科学基金青年科学基金项目(31301602);“十三五”国家重大科技专项(2016YFD0400400);哈尔滨市科技局科技创新人才研究专项资金项目(2016RAQXJ146).

摘　　要：使用傅里叶变换红外光谱技术对大豆蛋白-酪蛋白组装物的二级结构进行研究。组装物在酰胺Ⅰ带和Ⅲ带位置中各特征峰相互叠加,采用Gausses峰型对圆头峰进行拟合、解析,判断其α-螺旋,β-折叠,β-转角和无规则卷曲的相对含量。研究发现:酰胺Ⅰ带和酰胺Ⅲ带在数值上对CNPSPC的二级结构定量表现出差异性,而在pH对CNPSPC的β-折叠结构及α-螺旋结构的影响上表现一致,即随着p H值的增大,α-螺旋结构含量呈先降低后增加趋势,β-折叠含量呈现先增加后降低的趋势,且在pH 6.0时含量最大。The secondary structure of soybean-casein assembly was studied using Fourier transform infrared spectroscopy(FTIR) techniques. Due to the type of assembly product in amide Ⅰ belt and Ⅲ belt position, each characteristic peaks overlap, so the type of round head Gausses peak fitting, parsing, judge the α-helix, β-sheet, β-turn and Random coil relative content. It was found that amide Ⅰ was difference from amide Ⅲ to secondary structure quantitative of CNPSPC in the numerical. But the effect of p H on the β-folding and the α-helix structure of CNPSPC is consistent;With the increase of pH, The content of α-helix structure decreases and then increases. The content of the β-folding increases and then decreases, and when pH6.0 beta folding content is the largest.

关 键 词：大豆蛋白 酪蛋白 复合物 二级结构 傅里叶变换红外光谱 

分 类 号：TS201.21[轻工技术与工程—食品科学]