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Immobilized enzyme
About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.
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TL;DR: A simple preparation process was developed for magnetic nanoparticles, consisting of chitosan coated on Fe3O4 nanoparticle, to be used as support for enzyme immobilization.
Abstract: A simple preparation process was developed for magnetic nanoparticles, consisting of chitosan coated on Fe3O4 nanoparticles, to be used as support for enzyme immobilization. Cellulase was covalentl...
198 citations
TL;DR: It appears that the glass-enzyme complex developed in the present work can be used as a high-performance biocatalyst for various chemical processing applications, particularly in organic media.
Abstract: A unique nanoporous sol-gel glass possessing a highly ordered porous structure (with a pore size of 153 A in diameter) was examined for use as a support material for enzyme immobilization. A model enzyme, α-chymotrypsin, was efficiently bound onto the glass via a bifunctional ligand, trimethoxysilylpropanal, with an active enzyme loading of 0.54 wt%. The glass-bound chymotrypsin exhibited greatly enhanced stability both in aqueous solution and organic solvents. The half-life of the glass-bound α-chymotrypsin was >1000-fold higher than that of the native enzyme, as measured either in aqueous buffer or anhydrous methanol. The enhanced stability in methanol, which excludes the possibility of enzyme autolysis, particularly reflected that the covalent binding provides effective protection against enzyme inactivation caused by structural denaturation. In addition, the activity of the immobilized α-chymotrypsin was also much higher than that of the native enzyme in various organic solvents. From these results, it appears that the glass–enzyme complex developed in the present work can be used as a high-performance biocatalyst for various chemical processing applications, particularly in organic media. Published by John Wiley & Sons Biotechnol Bioeng 74: 249–255, 2001.
197 citations
TL;DR: These unique composite particles containing rGO and Fe3O4 may be promising supports for the efficient immobilization of industrially important enzymes with lower acute toxicity toward Vibrio fischeri than commercial pure Fe3 O4 particles.
Abstract: A novel type of spherical and porous composites were synthesized to dually benefit from reduced graphene oxide (rGO) and magnetic materials as supports for enzyme immobilization. Three magnetic composite particles of Fe3O4 and rGO containing 71% (rGO-Fe3O4-M1), 36% (rGO-Fe3O4-M2), and 18% (rGO-Fe3O4-M3) Fe were prepared using a one-pot spray pyrolysis method and were used for the immobilization of the model enzymes, laccase and horseradish peroxidase (HRP). The rGO-Fe3O4 composite particles prepared by spray pyrolysis process had a regular shape, finite size, and uniform composition. The immobilization of laccase and HRP on rGO-Fe3O4-M1 resulted in 112 and 89.8% immobilization efficiency higher than that of synthesized pure Fe3O4 and rGO particles, respectively. The stability of laccase was improved by approximately 15-fold at 25 °C. Furthermore, rGO-Fe3O4-M1-immobilized laccase exhibited 92.6% of residual activity after 10 cycles of reuse and was 192% more efficient in oxidizing different phenolic compou...
196 citations
TL;DR: This review summarizes the current state of knowledge regarding the materials used for enzyme immobilization of these oxidoreductase enzymes for environmental applications and provides an improved foundation on which new technological advancements can be made to achieve efficient enzyme-assisted bioremediation.
195 citations
TL;DR: The use of mesoporous molecular sieves in enzyme immobilisation has been studied in this article, where three different types of sieves (MCM-41, MCM-48 and SBA-15) were selected because of the differences in their pore dimensions and structures.
194 citations