FTIR, SEM and Fractal dimension characterization of of Lipase B from Candida Antactica B Immobilized onto Titania at Selected Conditions

MARIA LAURA FORESTI; GRACIELA M. VALLE; RITA D. BONETTO; MARÍA LUJAN FERREIRA; LAURA ESTEFANÍA BRIAND

APPLIED SURFACE SCIENCE

Elsevier

Lugar: North Holland; Año: 2010 vol. 256 p. 1624 - 1635

0169-4332

Lipase B from Candida antarctica was immobilized onto titanium dioxide. The dsorption isotherm was determined by UV-VIS analysis of supernatant solution at 280 nm, revealing that in seven hours 98% of the theoretic lipase monolayer was achieved. Samples withdrawn from the supernatant immobilization medium were analyzed by Fourier-transform infrared spectroscopy in the 1700 to 1600 cm-1 range (Amide I) in order to obtain quantitative information on the evolution of the secondary-structure elements that compose the protein. The analysis performed revealed that lipase conformation suffers only minor changes during its adsorption onto TiO2. Characterization of the immobilized biocatalyst implied SEM, AFM, fractal dimension analysis and FTIR techniques.