Title of article :
Binding and degradation of DNA on montmorillonite coated by hydroxyl aluminum species
Author/Authors :
Cai، نويسنده , , Peng and Huang، نويسنده , , Qiaoyun and Li، نويسنده , , Ming and Liang، نويسنده , , Wei، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Abstract :
Adsorption, desorption and degradation by DNase I of DNA on montmorillonite (M) and different hydroxyaluminum-M complexes (Al(OH)x-M) containing 2.5, 10.0 and 20.0 mmol coated Al/g clay (AM2.5, AM10 and AM20) were studied. The adsorption isotherms of DNA on montmorillonite and Al(OH)x-M complexes conformed to the Langmuir equation. The amount of DNA adsorbed followed the sequence of montmorillonite > AM20 > AM10 > AM2.5. A marked decrease in the adsorption of DNA on montmorillonite and Al(OH)x-M complexes was observed with the increase of pH from 4.0 to 9.0. Calcium ion significantly promoted DNA adsorption. The adsorption enthalpy of DNA on montmorillonite was endothermic, whereas that on Al(OH)x-M complexes was exothermic. The percent desorption of DNA from clays was in the order of montmorillonite > AM2.5 > AM10 > AM20, suggesting that OH–Al loading on montmorillonite surface increased the binding affinity of DNA. Fourier transform infrared (FTIR) spectra showed that the binding of DNA on AM10 and AM20 changed its conformation from the B-form to the Z-form. The presence of montmorillonite and Al(OH)x-M complexes provided protection for DNA against degradation by DNase I. The higher level of protection was found with Al(OH)x-M complexes compared to montmorillonite. The higher stability of DNA in the system of Al(OH)x-M complexes seemed to be attributed mainly to the conformational change of bound DNA and their greater adsorption capacity for DNase I. The information obtained in this study is of fundamental significance for understanding the behavior of extracellular DNA in soil environments.
Keywords :
Hydroxyl aluminum , Adsorption , Degradation , Microcalorimetry , DNA , Montmorillonite
Journal title :
Colloids and Surfaces B Biointerfaces
Journal title :
Colloids and Surfaces B Biointerfaces