Analysis of conditions for the preparation of BSA/MMT composites

Abstract This study describes a new method for protein fixation that has high, stable, and good repeatable fixation effect without deactivating protein. This method involves intercalating bovine serum albumin (BSA) into montmorillonite (MMT) under different experimental conditions, i.e., the concentration of coupling agent KH570, pH values, ionic strength, and the impact of buffers. The study showed the interaction of buffer systems with pH values had the most significant influence on adsorption quantity. The existence of the buffer increased the adsorption quantity and helped with slow protein releasing, while the phosphate buffer worked better than acetate buffer. More BSA was adsorbed on KH570 treated than untreated MMT, and among the treated samples the most protein released was on MMT treated with KH570 in 100% ethanol and in the acetate buffer solution. Adsorption quantity of the BSA initially increased and then decreased with the increase of the ionic strength. The research on the preparation of MMT/BSA materials provides further information on the study of protein composites.