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Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Catalytic properties of maltogenic α-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea)
Antanas Straksys1, Tatjana Kochane1, Saulute Budriene1
1Department of Polymer Chemistry, Vilnius University, Naugarduko 24, LT-03225 Vilnius, Lithuania.
Abstract:
The immobilization of maltogenic α-amylase from Bacillus stearothermophilus (BsMa) onto novel porous poly(urethane urea) (PUU) microparticles synthesized from poly(vinyl alcohol) and isophorone diisocyanate was performed by covalent attachment to free isocyanate groups from PUU microparticles, or by physical adsorption of enzyme onto the surface of the carrier. The influence of structure, surface area and porosity of microparticles on the catalytic properties of immobilized BsMa was evaluated. The highest efficiency of immobilization of BsMa was found to be 72%. Optimal activity of immobilized BsMa was found to have increased by 10°C compared with the native enzyme. Influence of concentration of sodium chloride on activity of immobilized BsMa was evaluated. High storage and thermal stability and reusability for starch hydrolysis of immobilized enzyme were obtained. Immobilized BsMa has a great potential for biotechnology.

