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作 者:贾娜尔.吐尔逊 王晓娅 谭瑞康[1] 李德强[1] TUERXUN Jianaer;WANG Xiaoya;TAN Ruikang;LI Deqiang(College of Chemical Engineering, Xinjiang Agricultural University, ürümqi 830052, China;Quality Control Department, Xinjiang Blue Ridge Tunhe Chemical Industry Joint Stock Co. Ltd., Changji 831800, China)
机构地区:[1]新疆农业大学化学工程学院,新疆乌鲁木齐830052 [2]新疆蓝山屯河能源有限公司质管部,新疆昌吉831800
出 处:《食品科学》2017年第15期183-188,共6页Food Science
基 金:新疆农业大学校前期资助课题(XJAU201204)
摘 要:以溴化1-乙基-3-甲基咪唑(1-ethyl-3-methylimidazolium bromide,[C2mim]Br)为原料,采用中和法合成氨基酸离子液体1-乙基-3-甲基咪唑-2-氨基-1,3-戊二酸盐(1-ethyl-3-methylimidazolium 1-aminopropane-1,3-dicarboxylic acid salt,[C2mim][Glu])。分别采用亲和毛细管电泳法和荧光猝灭法考察α-乳白蛋白与[C2mim][Glu]、α-乳白蛋白与[C2mim]Br的相互作用。结果得到二者结合常数均在10~6 L/mol量级,且α-乳白蛋白-[C2mim][Glu]的结合常数大于α-乳白蛋白-[C2mim]Br,结合比约为1∶1。实验结果为进一步研究α-乳白蛋白与离子液体相互作用机理、开发高效环境友好的α-乳白蛋白萃取体系具有一定的参考意义。An amino acid ionic liquid(AAIL),1-ethyl-3-methylimidazolium1-aminopropane-1,3-dicarboxylic acid salt([C2mim][Glu]),was synthesized by the neutralization method from1-ethyl-3-methylimidazolium bromide([C2mim]Br).The binding behavior ofα-lactalbumin(α-LAB)with[C2mim][Glu]and[C2mim]Br was evaluated by affinity capillary electrophoresis and fluorescence quenching method.The binding constants of bothα-LAB-[C2mim][Glu]andα-LAB-[C2mim]Br were in the order of magnitude of106L/mol,with the former being higher than the latter,and the binding ratios were approximately1:1.This research may provide some references for further studies aimed to understand the mechanism behindα-LAB-ionic liquid interaction and develop an efficient and environment-friendly extraction system forα-LAB.
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