辣条中糖精钠含量测定及其与牛血清白蛋白的相互作用  

Determination of Saccharin Sodium Content in Spicy Gluten and Spectroscopic Analysis on the Interaction of Saccharin Sodium with Bovine Serum Albumin

作　　者：顾佳丽[1] 李东玲 赵刚[1,2] 励建荣 Gu Jiali;Li Dongling;Zhao Gang;Li Jianrong(School of Chemistry ＆ Chemical Engineering, Bohai University, Jinzhou 121013, Liaoning;College of Food Science and Technology, Bohai University, Food Safety Key Lab of Liaoning Province, National ＆ Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, Jinzhou, 121013, Liaoning)

机构地区：[1]渤海大学化学化工学院,辽宁锦州121013 [2]渤海大学食品科学与工程学院辽宁省食品安全重点实验室生鲜农产品贮藏加工及安全控制技术国家地方联合工程研究中心,辽宁锦州121013

出　　处：《中国食品学报》2018年第5期257-263,共7页Journal of Chinese Institute Of Food Science and Technology

基　　金："十二五"国家科技支撑计划项目(2012BAD29B06);中央财政支持地方高校发展专项资金项目;辽宁高等学校攀登学者支持计划项目(辽教发[2011]134号);2015年地方高校辽宁省大学生创新创业训练计划项目(201510167000002)

摘　　要：采用高效液相色谱法测定市售辣条中糖精钠的含量,结果所测13种样品中有8种辣条糖精钠含量超过国家标准。采用荧光光谱法和紫外光谱法研究模拟生理条件下糖精钠与牛血清白蛋白(BSA)的相互作用机制。荧光猝灭试验结果表明:糖精钠和BSA复合物的形成导致BSA内源荧光的猝灭;根据Stern-Volmer方程,糖精钠对BSA的动态猝灭常数在温度298,303 K和310 K条件下分别为3.31×1012,2.99×1012和2.60×1012L/(mol·s);298 K时,其结合常数与结合位点数分别为2.74×108 L/mol和1.92;热力学参数熵变(ΔH)与焓变(ΔS)分别为-51.35 k J/mol和-10.76 J/mol,表明糖精钠与BSA之间的主要作用力为范德华力和氢键;依据F觟ster非辐射能量转移理论计算糖精钠与BSA间的结合距离为6.10 nm,两者之间极有可能发生非辐射能量转移现象,导致荧光猝灭。同步荧光光谱法和三维荧光光谱法结果表明:糖精钠引起BSA分子构象的变化。The saccharin sodium content of spicy gluten were determined by high performance liquid chromatography（HPLC）, the results indicated that among the 13 tested samples, 8 samples contained excessive levels of saccharin sodium. The interaction between saccharin sodium（SSA） and bovine serum albumin（BSA） under simulative physiological conditions was studied by fluorescence spectrum and UV-vis spectrum spectroscopy. The results indicated that the formation of SSA-BSA complex caused fluorescence quenching of BSA. The dynamic quenching constant at different temperatures were 3.31×1012, 2.99×1012 and 2.60×1012 L/（mol·s） respectively. The binding constant K between SSA and BSA was found to be 2.74×108 L/mol and the binding sites value n was 1.92 at 298 K. The entropy change（ΔH） and enthalpy change（ΔS） were calculated to be-51.35 k J/mol and-10.76 J/mol, revealing that the interaction of SSA and BSA were van der Waals forces and hydrogen bonds. The distance r between SSA and BSA was 6.10 nm based on F觟ster＇s non-radiative energy transfer theory. The results of synchronous fluorescence and three-dimensional fluorescence indicated that the conformation of BSA was changed with the addition of SSA.

关 键 词：辣条 糖精钠 牛血清白蛋白 

分 类 号：TS207.3[轻工技术与工程—食品科学]