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Selective Desorption of Intercalated Bovine Serum Albumin and Lysozyme by Organically Modified Montmorillonite
Author(s) -
Tsai TsungYen,
Hsu ChaoChen,
Chao Wu Victor WeiKeh,
Huang SinHsin,
Chan Chieh,
Wu TiChia,
Wang PingHan
Publication year - 2015
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201400503
Subject(s) - chemistry , montmorillonite , lysozyme , bovine serum albumin , desorption , adsorption , chromatography , sodium dodecyl sulfate , gel electrophoresis , polyacrylamide gel electrophoresis , electrophoresis , serum albumin , nuclear chemistry , organic chemistry , biochemistry , enzyme
The organically modified montmorillonite (M‐Mt) was applied as an adsorbent for the purification of bovine serum albumin (BSA). In order to differentiate the selectivity and perform the purification of BSA, two kinds of proteins, BSA and lysozyme (LYZ) were mixed together and prepared at different pH, which could change the electrical charges on the surfaces of the proteins. BSA and LYZ can be adsorbed at the lower pH into the organically modified montmorillonite, which could be confirmed by powder X‐ray diffraction (XRD) in the d‐value increased after the adsorption of proteins. However, there is only BSA desorption was observed, approved by the method of Sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis (PAGE), from this adsorbed protein mixture when the pH of the solution was adjusted and optimized. These results indicate that there is electrostatic interaction between a suitably modified montmorillonite and proteins BSA and LYZ to perform the selective desorption from BSA in the mixture of these proteins.