Immobilized enzymes: understanding enzyme - surface interactions at the molecular level
Enzymes immobilized on solid supports have important and industrial and medical applications. However, their uses are limited by the significant reductions in activity and stability that often accompany the immobilization process. Here we review recent advances in our understanding of the molecular...
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| Published in | Organic & biomolecular chemistry Vol. 15; no. 45; pp. 9539 - 9551 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Royal Society of Chemistry
22.11.2017
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| Subjects | |
| Online Access | Get full text |
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| Summary: | Enzymes immobilized on solid supports have important and industrial and medical applications. However, their uses are limited by the significant reductions in activity and stability that often accompany the immobilization process. Here we review recent advances in our understanding of the molecular level interactions between proteins and supporting surfaces that contribute to changes in stability and activity. This understanding has been facilitated by the application of various surface-sensitive spectroscopic techniques that allow the structure and orientation of enzymes at the solid/liquid interface to be probed, often with monolayer sensitivity. An appreciation of the molecular interactions between enzyme and surface support has allowed the surface chemistry and method of enzyme attachement to be fine-tuned such that activity and stability can be greatly enhanced. These advances suggest that a much wider variety of enzymes may eventually be amenable to immobilization as green catalysts.
Interactions between immobilized enzymes and supporting surfaces are complex and context-dependent and can significantly alter enzyme structure, stability and activity. |
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| Bibliography: | Marie Hoarau completed her Master degree in Molecular Chemistry in Université Pierre et Marie Curie (Paris, France). She obtained her PhD in 2016 from Université Paul Sabatier (Toulouse, France) under the guidance of Dr Emmanuel Gras and Prof. Magali Remaud-Siméon, working on the development of new bioinorganic catalysts made of coordination complexes supported on amyloid fibres. In 2017, she joined Prof. Neil Marsh's research group, working on the development of novel immobilized enzyme-based systems for the detection and degradation of pollutants. Somayesadat Badieyan received her master degree in Biotechnology minoring in Biochemical Sciences and Engineering from University of Tehran, Iran. In 2012, she earned her Ph.D. in Biological Engineering under the direction of Dr Mike Zhang and David Bevan from Virginia Tech (Blacksburg, VA) where she investigated thermal stability of glycoside hydrolases using Molecular Dynamics and designed cellulases with enhance activity and stability. She is currently a postdoctoral researcher at Department of Chemistry, University of Michigan and works with Prof. Neil Marsh on activation of surface tethered enzymes in the water-free environments. She is also working on symmetry-based design of protein cages. Neil Marsh is Professor of Chemistry and Biological Chemistry at the University of Michigan. His group works on a variety of projects in the fields of enzymology and protein engineering. Current research interests include: understanding how enzyme-surface interactions alter enzyme structure, stability and activity; the applications of immobilized enzymes as sensors and biocatalysts; the role of radical SAM enzymes in the cellular antiviral response; mechanisms of enzymes involved in hydrocarbon biosynthesis; and the design of modular self-assembling protein cages. ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
| ISSN: | 1477-0520 1477-0539 |
| DOI: | 10.1039/c7ob01880k |