Mesoporous silica particles were prepared by the sol-gel method from
different alkoxysilane precursors and used as a host matrix for encapsulation
of glucoamylase, an enzyme widely used in fermentative industry. The aim was
to investigate the physico-chemical properties of the different silica
powders and their effect on the enzyme kinetics. The encapsulated enzymes
followed Michaelis-Menten kinetics. The Michaelis constant (KM) and the
maximum rate of starch hydrolysis reaction (Vmax) were calculated according
to the Michaelis-Menten and Lineweaver-Burke plots. The values of the
Michaelis constant (KM) of the encapsulated enzymes were higher than those of
the free enzyme. The temperature and pH influence on the activity of free and
immobilized glucoamylase were also compared. The results of this study show
that the enzymes immobilized in organic/inorganic hybrid silica matrixes
(obtained by the sol-gel method), allowing the entrapped glucoamylase to
retain its biological activity, are suitable for many different applications,
(medicinal, clinical, analytical).
Entrapment of glucoamylase by sol-gel technique in PhTES/TEOS hybrid matrixes