Search results for "Immobilized enzyme"
showing 6 items of 16 documents
Encapsulation of cytochrome C by multilayer microcapsules. A model for improved enzyme immobilization
1997
Cytochrome C was used as a model compound to study the behavior of proteins during the encapsulation procedure in alginate microcapsules and the loss by diffusion during storage. Alginate gel beads were coated with a multilayer membrane consisting of alternating layers of poly(N-vinylamine) and poly(acrylic acid) or water soluble anionic cellulose derivatives, respectively. To obtain high encapsulation yields, it is recommended to use the lowest possible concentration of salts in the precipitation bath. Loss during storage (and use) is minimized by applying at least two polycation/polyanion double layers for the membrane. Cellulose derivatives are superior over poly(acrylic acid). Single la…
Fabrication of a Silica Coating on Magnetic γ-Fe2O3 Nanoparticles by an Immobilized Enzyme
2008
Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe2O3) nanoparticles that were surface functionalized with a reactive mulfunctional polymer. This polymer carries an anchor group based on dopamine which is capable of binding to the γ-Fe2O3 surface and a reactive functional group which allows binding of various biomolecules onto inorganic nanoparticles. This functional nitrilotriacetic acid (NTA) group allows immobilization of His-tagged silicatein on the surface of the γ-Fe2O3 nanoparticles. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica through copolymerization of alkoxysilanes Si(OR)4. Functio…
Enzyme-modified electrodes for biosensors and biofuel cells
2019
In biosensors and biofuel cells, it is often desirable to accelerate the electron transfer rate between the enzyme and electrode surface to improve the performance of the devices (sensitivity or power output). To this end, in this review, we focus on three important strategies available to improve the performance of enzyme-modified electrodes: the use of protein engineering, designer polymers, and the introduction of nanomaterials. Engineering the protein or proteins that constitute the biocatalytic elements allow tuning their stability, activity, and specificity. It can also allow changing the enzyme immobilization efficiency (adsorption vs. covalent immobilization, for example). If direct…
Immobilization of enzymes by multilayer microcapsules
1994
A method is described to obtain a new type of microcapsules for immobilization of enzymes or living cells. The wall of these capsules consists of several layers of poly(ethyleneimine) and poly(acrylic acid). The idea is that diverging properties of the whole assembly can be better controlled when the membrane is built up by several consecutive steps, each being optimized with respect to a special property, for example, permeability or mechanical strength. The encapsulation of acidic phosphatase and the cleavage of p-nitrophenyl phosphate was used as a model system. The charged capsules were characterized by their enzymatic activity, as a function of membrane composition (number and sequence…
Hydrogen peroxide sensing with horseradish peroxidase-modified polymer single conical nanochannels.
2011
Inspired from the funtioning and responsiveness of biological ion channels, researchers attempt to develop biosensing systems based on polymer and solid-state nanochannels. The applicability of these nanochannels for detection/sensing of any foreign analyte in the surrounding environment depends critically on the surface characteristics of the inner walls. Attaching recognition sites to the channel walls leads to the preparation of sensors targeted at a specific molecule. There are many nanochannel platforms for the detection of DNA and proteins, but only a few are capable of detecting small molecules. Here, we describe a nanochannel platform for the detection of hydrogen peroxide, H(2)O(2)…
Chemie an starren Grenzflächen, 10. Kinetisches Verhalten einiger an „Isothiocyanato-Aerosil” immobilisierter Esterasen – Analogversuche mit Insulin
1988
Amino-Aerosil wird mit Thiophosgen nach Gl. (1) in Isothiocyanato-Aerosil 2 (NCS-Aerosil) ubergefuhrt. Trypsin, Cholinesterase und Acetylcholinesterase werden an 2 nach Gl. (2) immobilisiert. Die Aktivitat der immobilisierten Esterasen wird untersucht auf (a) Lagerstabilitat, (b) Temperaturbestandigkeit und (c) pH-Abhangigkeit. Das kinetische Verhalten der immobilisierten Enzyme wird verglichen mit dem der freien, aber mit n-Butylisothiocyanat behandelten Esterasen. Am Beispiel der Cholinesterase, die uber unterschiedliche Ankergruppen mit Aerosil verknupft wurde, wird der Einflus unterschiedlicher Spacergruppen auf die Hydrolysegeschwindigkeit studiert. Aerosile, die mit Acetylcholin-Analo…