Structural and viscoelastic properties of floating monolayers of a pectinolytic enzyme and their influence on the catalytic properties

Abstract

Hypothesis: The catalytic activity of enzymes immobilized in self-assembly systems as Langmuir-Blodgett (LB) films is influenced by molecular interactions dictated by the composition and viscoelasticity of the previous floating monolayers. We believe that the insertion of carbon nanotubes (CNT) in mixed polygalacturonase/lipid monolayers may influence intermolecular interactions and viscoelastic properties, being then possible to tune system stability and rheological properties, driving catalytic properties of the films for biosensing.

Experiments: The physicochemical properties of the monolayers were investigated by tensiometry, surface potential, Brewster angle microscopy, infrared spectroscopy, and dilatational rheology. The monolayers were transferred to solid supports LB films and characterized by atomic force microscopy, quartz crystal microbalance, and fluorescence spectroscopy. The catalytic activity of the LB films was verified by colorimetric assay.

Findings: The enzyme-CNT-lipid film had a catalytic activity at least twice as high as the pure enzyme owing to the synergy between the components, with the lipid acting as a protector matrix for the enzyme and the CNTs acting as an energy transfer facilitator. These results point to a proof-of-concept system, through which we can propose an alternative to achieve enhanced bio-inspired films with high control of the molecular architecture by using the LB approach.

Keywords: Carbon nanotubes; Enzyme; LB films; Pectin; Pectinase.