ABSTRACT: The present work describes the immobilization of α-amylase over well ordered mesoporous molecular sieve SBA-15 with different
pore diameters synthesized by post synthesis treatment (PST) hydrothermally after reaction at 40°C. The materials were characterized
by N2 adsorption–desorption studies, small angle X-ray diffraction, scanning electron microscopy and high resolution transmission
electron microscopy. Since α-amylase obtained from Bacillus subtilis has dimensions of 35×40×70Å it is expected that the protein have access to the pore of SBA-15 (PST-120°C) with diameter
74Å. 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.
Journal of Porous Materials 04/2012; 17(3):341-349. · 1.24 Impact Factor