Title of article :
Improvement of thermal stability of enzyme via immobilization on Langmuir–Blodgett films of organo-modified aluminosilicate with high coverage
Author/Authors :
Fujimori، نويسنده , , Atsuhiro and Arai، نويسنده , , Shuntaro and Soutome، نويسنده , , Youichi and Hashimoto، نويسنده , , Masamichi، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2014
Pages :
8
From page :
45
To page :
52
Abstract :
Ultrathin films of regularly adsorbed biological molecules have been fabricated by means of the modified Langmuir–Blodgett (LB) method using an organo-modified aluminosilicate (montmorillonite). In this combined method, clay LB films play a template role in the formation of the lysozyme thin layer. Chemisorption of biological molecules to the anionic montmorillonite (MMT) surface was confirmed by a comparison between infrared spectra of multilayers of organo-clay and of chemisorbed lysozyme. The surface morphology of these monolayers was observed by atomic force microscopy. In the case of organo-modified aluminosilicate, it is also indicated that chemisorbed enzyme activity is possible to maintain until 160 °C at attempting to evaluation of the heat-resistance. The maintaining of enzyme activity at high temperature region is possible together with the maintaining of three-dimensional steric structure of enzyme. This maintaining of steric structure of enzyme is based on the formation of aggregate of adsorbed enzyme induced by epitaxial-growth from aluminosilicate surface and the construction of sandwiched structure of enzyme between organo-aluminosilicates.
Keywords :
Langmuir–Blodgett films , Lysozyme , Organo-modified aluminosilicate , Electrostatic Interaction , Molecular arrangement
Journal title :
Colloids and Surfaces A Physicochemical and Engineering Aspects
Serial Year :
2014
Journal title :
Colloids and Surfaces A Physicochemical and Engineering Aspects
Record number :
1945970
Link To Document :
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