
%0 Journal Article
%A Simpson, GH 
%A Hughes, JD 
%T Arylsulphatase clay interactions. I. Adsorption of arylsulphatase by kaolinite and montmorillonite
%J Soil Research
%D 1978/04/01
%V 16
%N 1
%P 27-33
%K 
%R https://doi.org/10.1071/SR9780027
%U https://www.publish.csiro.au/paper/SR9780027 
%X The extent of arylsulphatase adsorption by both montmorillonite and kaolinite was determined using 0.1-1.0 µm 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. 
