Tuning mesoporous molecular sieve SBA-15 for the immobilization of α-amylase

The present work describes the immobilization of alpha-amylase over well ordered mesoporous molecular sieve SBA-15 with different pore diameters synthesized by post synthesis treatment (PST) hydrothermally after reaction at 40A degrees C. The materials were characterized by N-2 adsorption-desorption studies, small angle X-ray diffraction, scanning electron microscopy and high resolution transmission electron microscopy. Since alpha-amylase obtained from Bacillus subtilis has dimensions of 35 x 40 x 70 a<< it is expected that the protein have access to the pore of SBA-15 (PST-120A degrees C) with diameter 74 a<<. The pore dimension is appropriate to prevent considerable leaching. The rate of adsorption of the enzyme on silica of various pore sizes revealed the influence of morphology, pore diameter, pore volume and pH.