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Cited by 521

The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.

Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases

Open access
Guzik, Urszula, Hupert-Kocurek, Katarzyna, Wojcieszyńska, Danuta·2014·Molecules

Abstract

The main objective of the immobilization of enzymes is to enhance the economics of biocatalytic processes. Immobilization allows one to re-use the enzyme for an extended period of time and enables easier separation of the catalyst from the product. Additionally, immobilization improves many properties of enzymes such as performance in organic solvents, pH tolerance, heat stability or the functional stability. Increasing the structural rigidity of the protein and stabilization of multimeric enzymes which prevents dissociation-related inactivation. In the last decade, several papers about immobilization methods have been published. In our work, we present a relation between the influence of immobilization on the improvement of the properties of selected oxidoreductases and their commercial value. We also present our view on the role that different immobilization methods play in the reduction of enzyme inhibition during biotechnological processes.

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Crossref · 10.3390/molecules19078995

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Metadata

Authors
Guzik, U., Hupert-Kocurek, K., & Wojcieszyńska, D.
Venue
Molecules
Publisher
MDPI AG
Published
2014-06-27
Volume
19
Issue
7
Pages
8995-9018
ISSN
1420-3049 (ISSN-L)
OpenAlex
W1986159961
Cited by
521
References
75
FWCI
15.57
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases. https://app.cochat.ai/papers/10.3390/molecules19078995
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Guzik, U., Hupert-Kocurek, K., & Wojcieszyńska, D. (2014). Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases. Molecules. https://doi.org/10.3390/molecules19078995

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.