IMMOBILIZATION OF HORSERADISH PEROXIDASE ON SUGARCANE BAGASSE

The immobilization of horseradish peroxidase (HRP) on raw and alkaline pre-treated sugarcane bagasse by physical adsorption (ADS) and covalent bond (LC) methods was studied. The saturation of the support with 2 mg of HRP/g of support by LC immobilization reached 35% of immobilization efficiency and 39 units of the immobilized enzyme (U). Regarding the HRP immobilization on sugarcane bagasse without pretreatment and using the same HRP loading, it was observed a reduction in the efficiency of immobilization and in the number of immobilized units for both methods, ADS (13.98% and 15.46 U) and LC (15.79% and 17.46 U). The sugarcane bagasse with alkaline pretreatment experiment, on the other hand, exhibited higher potential for HRP immobilization by LC. The supports and biocatalysts were characterized by Fourier transform infrared spectroscopy (FTIR), showing greater availability of hydroxyl groups in the pretreated support and the typical amide I and amide II bands that corroborate the effectiveness of the enzyme immobilization on sugarcane bagasse. In the same way, the thermogravimetric analysis (TGA) confirmed a higher weight loss in the region I for the derivative immobilized by LC, suggesting the presence of water favored enzymatic activity.