Adsorption of the phosphotriesterase on a polysulfone membrane surface was investigated in this paper through a double-scale computational approach. Surface charges of the enzyme, as well as membrane, were calculated at sub and nanoscale while protein adsorption was simulated at larger scale. Adsorption energies were calculated as a function of the enzyme-surface distance, and for each distance, several protein rotations were tested to find the most stable orientations of the macromolecule. The results of this model were useful in obtaining information about the 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 enzymes due to the steric hindrance of the polymer surface; thus, a reduction of its eciency 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.

Enzyme immobilization on polymer membranes: A quantum and molecular mechanics study

Petrosino F.
;
Curcio S.;Chakraborty S.;
2019

Abstract

Adsorption of the phosphotriesterase on a polysulfone membrane surface was investigated in this paper through a double-scale computational approach. Surface charges of the enzyme, as well as membrane, were calculated at sub and nanoscale while protein adsorption was simulated at larger scale. Adsorption energies were calculated as a function of the enzyme-surface distance, and for each distance, several protein rotations were tested to find the most stable orientations of the macromolecule. The results of this model were useful in obtaining information about the 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 enzymes due to the steric hindrance of the polymer surface; thus, a reduction of its eciency 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.
Density functional theory; Double-scale computational modeling; Enzyme adsorption and orientation; Polysulfone membrane
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.11770/304507
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 11
  • ???jsp.display-item.citation.isi??? 11
social impact