How a crosslinker agent interacts with the β-glucosidase enzyme surface in an aqueous solution: Insight from quantum mechanics calculations and molecular dynamics simulations.

摘要: Abstract In this study, surficial interactions of glutaraldehyde (GA) as an important crosslinker agent with the β-glucosidase (BGL) enzyme surface were investigated by theoretical methods. Since inherent constraints experimental methods limit their application to find molecular perspective these significant in immobilization, used a complementary tool understand concept. The Minnesota density functional calculations showed that chair conformations oxane-2,6-diol form GA more stable than its free aldehyde form. MD simulations propylamine-GA molecules, representative attached-GA, aqueous solutions different concentrations done determine basis BGL surface. root mean square fluctuation (RMSF) demonstrated maximum flexibility belonged 460–480 residues all solutions. Based on spatial distribution function (SDF) analysis, active site entrance was most favored region accumulate solute molecules. Radial (RDF) results forms molecules interacted from head side lysine BGL, which Lys247, Lys376, and Lys384 found be interactive residues. Also, hydrogen bond (HB) analysis two viewpoints confirmed HB formation possibility between These explained regions have interact link help us understanding process immobilization.