Abstract
Protein-montmorillonite composites were prepared by direct and stepwise intercalation of lysozyme(LYZ) into gallery of montmorillonite(MMT), and characterized by X-ray Diffraction (XRD), Thermal Gravimetric Analysis(TGA) and Atomic Force Microscopy(AFM). The direct intercalation experiment showed that with the increase of LYZ/MMT weight ratio from 1:1 to 4:1, the interlayer space of MMT increased from 4.2nm to 6.3nm, and the adsorption amount of lysozyme onto MMT increased from 1.05mg/mg to 1.84mg/mg. While in stepwise intercalation process, the adsorption of LYZ was obviously lower than that in direct intercalation experiment, indicating that the exchange reaction between lysozyme and POP-D2000 was incomplete in the stepwise intercalation reaction.
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