Abstract
The extent of arylsulphatase adsorption by both montmorillonite and kaolinite was determined using 0.1-1.0 �m fraction of sodium-clay freed from organic material, and a commercially purified arylsulphatase. Kaolinite-arylsulphatase affinity decreased with increasing solution enzyme concentration, but montmorillonitearylsulphatase affinity increased up to a solution enzyme concentration of approximately 15 mg/100 mg of clay, and decreased at higher enzyme concentrations. X-ray diffraction of the montmorillonite-arylsulphatase complex provided evidence of intercalation of the enzyme in the 2:1 lattice structure, as well as destruction of secondary and tertiary structures of the enzyme following adsorption on the interlattice surfaces.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
