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

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.

Carbon Nanotubes and Algal Polysaccharides To Enhance the Enzymatic Properties of Urease in Lipid Langmuir-Blodgett Films.

Algal polysaccharides (extracellular polysaccharides) and carbon nanotubes (CNTs) were adsorbed on dioctadecyldimethylammonium bromide Langmuir monolayers to serve as a matrix for the incorporation of urease. The physicochemical properties of the supramolecular system as a monolayer at the air-water interface were investigated by surface pressure-area isotherms, surface potential-area isotherms, interfacial shear rheology, vibrational spectroscopy, and Brewster angle microscopy. The floating monolayers were transferred to hydrophilic solid supports, quartz, mica, or capacitive electrolyte-insulator-semiconductor (EIS) devices, through the Langmuir-Blodgett (LB) technique, forming mixed films, which were investigated by quartz crystal microbalance, fluorescence spectroscopy, and field emission gun scanning electron microscopy.