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High Activity of Enzymes Immobilized in Colloidal Nanoreactors

✍ Scribed by Thorsten Neumann; Björn Haupt; Matthias Ballauff


Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
114 KB
Volume
4
Category
Article
ISSN
1616-5187

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✦ Synopsis


Abstract

Summary: We present a novel type of nanoreactor suitable for the immobilization of enzymes. The particles used consist of a polystyrene core onto which long chains of poly(acrylic acid) are grafted (“spherical polyelectrolyte brush”). Proteins adsorbed spontaneously onto these particles from aqueous solutions if the ionic strength is low. We immobilized glucoamylase on these particles and showed that this enzyme keeps nearly its full activity. This is shown by analyzing the enzymatic activity in terms of the Michaelis‐Menten kinetics. No leaching out of the enzyme takes place during the reaction and the colloidal stability is not impeded by the adsorbed biomolecules. The data presented here suggest that the principle of immobilizing enzymes on these particles may be of general use.

The Figure shows a schematic representation of the colloidal nanoreactors.

imageThe Figure shows a schematic representation of the colloidal nanoreactors.


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✍ Bruce P. Wasserman; Herbert O. Hultin; Bruce S. Jacobson 📂 Article 📅 1980 🏛 John Wiley and Sons 🌐 English ⚖ 725 KB

## Abstract Two types of polyethylenimine‐coated glass microbeads (13–44 μm) were synthesized and used for the immobilization of glucose oxidase from __Aspergillus niger__ and catalase from __A. niger__ and beef liver. The two types of beads were distinguishable by differences in their surface topo