Adsorption of phosphotriesterase enzymes on polysulfone membrane surface was investigated through a double-scale computational approach. Surface charges of enzyme as well as membrane were calculated at sub-nanoscopic and nanoscopic scales, whilest protein adsorption was simulated at a bigger scale. Adsorption energies were calculated as a function of the enzyme-surface distance and, for each distance, several protein rotations were tested in order to find the most stable orientations of the macromolecule. The results of this model were useful to obtain information about adhesion of the enzyme and to give indications on the orientations of its binding site. Adsorption energies agreed with the literature data. Furthermore the binding site of the immobilized phosphotriesterase was less accessible with respect to native enzyme due to the steric hindrance of the polymer surface; thus, a reduction of its efficiency is expected. The proposed methodology made use of fundamental quantities, calculated without resorting to adjustable or empirical parameters, providing basic outputs useful for ascertaining enzymatic catalysis rate.

Immobilization of enzymes on polymeric membranes: Quantum and molecular mechanics study

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.