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Tropine‐Based Ionic Liquid Gel for Adsorption of Protein Ovalbumin: High Capacity, Selectivity and Biocompatibility
Author(s) -
Li Fulin,
Lin Min,
Yao Shun,
Wang Xuejiao,
Zhu Minghui,
Song Hang
Publication year - 2020
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.202002072
Subject(s) - ovalbumin , lysozyme , egg white , adsorption , biocompatibility , chemistry , circular dichroism , differential scanning calorimetry , protein adsorption , salting out , ionic liquid , kinetics , chromatography , organic chemistry , crystallography , biochemistry , aqueous solution , catalysis , biology , immunology , physics , immune system , quantum mechanics , thermodynamics
Chicken ovalbumin (OVA) and lysozyme (LZ) are important biological products, which come from the egg‐white. However, the separation of OVA and LZ is realized by traditional salting‐out method needing large amount of ammonium sulfate, leading to lysozyme enzyme activity reducing. In this work, we used a tropine‐based ionic liquid (IL) hydrogel to separate OVA and LZ. The adsorption isotherms, thermodynamics and kinetics were investigated. The IL gel showed maximum adsorption capacity of 926 mg g −1 for OVA, nearly 152 % higher than that reported in other literature. Moreover, the secondary structure of desorbed OVA was confirmed by fluorescence spectroscopy (FL), circular dichroism spectra (CD) and differential scanning calorimetry (DSC). The material presented high OVA adsorption capacity, excellent OVA selectivity and good biocompatibility in OVA‐LZ protein system. It could be considered as a promising material for preferential protein adsorption, at least for separation of OVA and LZ.