Enzymes as tools in MIP-sensors
- Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences.
Author details: | Aysu YarmanORCiDGND, Katharina J. JetzschmannORCiD, Bettina NeumannORCiD, Xiaorong ZhangGND, Ulla WollenbergerORCiDGND, Aude Cordin, Karsten Haupt, Frieder W. SchellerORCiDGND |
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URN: | urn:nbn:de:kobv:517-opus4-474642 |
DOI: | https://doi.org/10.25932/publishup-47464 |
ISSN: | 1866-8372 |
Title of parent work (German): | Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe |
Publication series (Volume number): | Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (1098) |
Publication type: | Postprint |
Language: | English |
Date of first publication: | 2021/01/15 |
Publication year: | 2017 |
Publishing institution: | Universität Potsdam |
Release date: | 2021/01/15 |
Tag: | enzymatic MIP synthesis; enzymatic analyte conversion; enzyme tracer; molecularly imprinted polymers; template digestion |
Issue: | 1098 |
Number of pages: | 18 |
Source: | Chemosensors 5(2017) 2, 11; DOI: 10.3390/chemosensors5020011 |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
DDC classification: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
Peer review: | Referiert |
Publishing method: | Open Access / Green Open-Access |
License (German): | CC-BY - Namensnennung 4.0 International |
External remark: | Bibliographieeintrag der Originalveröffentlichung/Quelle |