FOOD SCIENCE ›› 2017, Vol. 38 ›› Issue (15): 183-188.doi: 10.7506/spkx1002-6630-201715030

• Basic Research • Previous Articles     Next Articles

Interactions of α-Lactalbumin with Ionic Liquids Analyzed by Affinity Capillary Electrophoresis and Fluorescence Quenching Method

TUERXUN Jianaer, WANG Xiaoya, TAN Ruikang, LI Deqiang   

  1. (1. College of Chemical Engineering, Xinjiang Agricultural University, ürümqi 830052, China; 2. Quality Control Department, Xinjiang Blue Ridge Tunhe Chemical Industry Joint Stock Co. Ltd., Changji 831800, China)
  • Online:2017-08-15 Published:2017-09-06

Abstract: An amino acid ionic liquid (AAIL), 1-ethyl-3-methylimidazolium 1-aminopropane-1,3-dicarboxylic acid salt ([C2mim][Glu]), was synthesized by the neutralization method from 1-ethyl-3-methylimidazolium bromide ([C2mim]Br). The binding behavior of α-lactalbumin (α-LAB) with [C2mim][Glu] and [C2mim]Br was evaluated by affinity capillary electrophoresis and fluorescence quenching method. The binding constants of both α-LAB-[C2mim][Glu] and α-LAB-[C2mim]Br were in the order of magnitude of 106 L/mol, with the former being higher than the latter, and the binding ratios were approximately 1:1. This research may provide some references for further studies aimed to understand the mechanism behind α-LAB-ionic liquid interaction and develop an efficient and environment-friendly extraction system for α-LAB.

Key words: α-lactalbumin (α-LAB), amino acid ionic liquids (AAIL), affinity capillary electrophoresis (ACE), binding constant, fluorescence quenching method

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