Abstract
An immobilization protocol of a model enzyme into silica nanoparticles was applied. This protocol exploited the use of the bifunctional molecule triethoxysilylpropylisocyanate (TEPI) for covalent binding through a linker of suitable length. The enzyme β-glucosidase (BG) was anchored onto wrinkled silica nanoparticles (WSNs). BG represents a bottleneck in the conversion of lignocellulosic biomass into biofuels through cellulose hydrolysis and fermentation. The key aspect of the procedure was the use of an organic solvent (anhydrous acetone) in which the enzyme was not soluble. This aimed to restrict its conformational changes and thus preserve its native structure. This approach led to a biocatalyst with improved thermal stability, characterized by high immobilization efficiency and yield. It was found that the apparent KM value was about half of that of the free enzyme. The Vmax was about the same than that of the free enzyme. The biocatalyst showed a high operational stability, losing only 30% of its activity after seven reuses.
Highlights
Enzymes are catalysts with excellent properties and high activity, selectivity, and specificity
BG represents a bottleneck in the conversion of lignocellulosic biomass into biofuels through cellulose hydrolysis and fermentation
The covalent immobilization protocol led to a biocatalyst with high activity, immobilization yield, thermal stability, and reusability
Summary
Enzymes are catalysts with excellent properties and high activity, selectivity, and specificity. The aim of this study is the development of an immobilization protocol through covalent binding of a model enzyme into silicate porous nanoparticles using the bifunctional molecule triethoxysilylpropylisocyanate (TEPI) This methodology is based on the use of an organic solvent (anhydrous acetone) in which the enzyme is insoluble so to restrict its conformational freedom and preserve its native structure. This should reduce the enzyme inactivation and greatly increase its stability. The covalent immobilization protocol led to a biocatalyst with high activity, immobilization yield, thermal stability, and reusability
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