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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: It is demonstrated that the enzymatic route is viable in scCO2, yielding poly(e-caprolactone) with molecular weights very similar to those obtained from the same enzyme catalysts in organic solvents, but with lower polydispersities and higher yields of polymer product.
Abstract: We report the ring-opening polymerization reaction of e-caprolactone in supercritical carbon dioxide (scCO2) using an enzyme catalyst, Lipase B from Candida antarctica supported on macroporous beads (Novozym-435). Ring-opening polymerization of lactones is more commonly performed in organic solvents or in bulk using a Lewis acid catalyst. Recently there has been much interest in the replacement of such catalysts by enzymes. We demonstrate that the enzymatic route is viable in scCO2, yielding poly(e-caprolactone) (Mn = 12 000−37 000 g mol-1) with molecular weights very similar to those obtained from the same enzyme catalysts in organic solvents, but with lower polydispersities (typical PDI = 1.4−1.6) and higher yields of polymer product (typically 95−98%). In the same process the unique “gaslike” mass transfer properties of scCO2 can also be exploited to remove quantitatively any unconverted monomer and low molecular weight oligomers by scCO2 extraction. It is also shown that the enzyme catalyst can be cle...
115 citations
TL;DR: Electrodeposition was used for the codeposition of glucose oxidase enzyme and a gold nanoparticle-silicate network onto an indium tin oxide (ITO) glass electrode, which imparts biocatalytic activity to the film.
Abstract: Electrodeposition was used for the codeposition of glucose oxidase enzyme and a gold nanoparticle–silicate network onto an indium tin oxide (ITO) glass electrode. This co-entrapment of glucose oxidase enzyme in a gold nanoparticle–silicate network imparts biocatalytic activity to the film. The gold nanoparticles in the network catalyse the oxidation and reduction of H2O2, the by-product of the enzymatic reaction. The low operating potential of the sensor eliminates the interference from common interferents, such as acetaminophen, ascorbic acid, dopamine, etc.
115 citations
TL;DR: A carbon electrode designed to achieve efficient enzymatic electrolysis by exploiting a hierarchical pore structure based on macropores for efficient mass transfer and mesopores for high enzyme loading is introduced.
Abstract: This article introduces a carbon electrode designed to achieve efficient enzymatic electrolysis by exploiting a hierarchical pore structure based on macropores for efficient mass transfer and mesopores for high enzyme loading. Magnesium oxide-templated mesoporous carbon (MgOC, mean pore diameter 38 nm) was used to increase the effective specific surface area for enzyme immobilization. MgOC particles were deposited on a current collector by an electrophoretic deposition method to generate micrometer-scale macropores to improve the mass transfer of glucose and electrolyte (buffer) ions. To create a glucose bioanode, the porous-carbon-modified electrode was further coated with a biocatalytic hydrogel composed of a conductive redox polymer, deglycosylated flavin adenine dinucleotide-dependent glucose dehydrogenase (d-FAD-GDH), and a cross-linker. Carbohydrate chains on the peripheral surfaces of the FAD-GDH molecules were removed by periodate oxidation before cross-linking. The current density for the oxidati...
115 citations
TL;DR: A method has been developed to remove the excess pyruvate effectively by complexation with bisulfite, thus allowing Neu5Ac to be recovered by absorption onto an anion-exchange resin and shows the importance of integrated process solutions for the effective scale-up of biotransformation reactions.
114 citations
TL;DR: In this paper, two synthetically useful glycosidases, the β-galactosidase from Bacillus circulans and an α-galacticase from Aspergillus oryzae have been immobilized on Eupergit C. They retain high catalytic activity and show increased thermal stability compared with the free enzymes.
114 citations