Abstract
The integration of enzymes with solid materials is important in many biotechnological applications, including the use of immobilized enzymes for biocatalytic synthesis. The development of functional enzyme-material composites is restrained by the lack of molecular-level insight into the behavior of enzymes in confined, surface-near environments. Here, we review recent advances in surface-sensitive spectroscopic techniques that push boundaries for the determination of enzyme structure and orientation at the solid-liquid interface. We discuss recent evidence from single-molecule studies showing that analyses sensitive to the temporal and spatial heterogeneities in immobilized enzymes can succeed in disentangling the effects of conformational stability and active-site accessibility on activity. Different immobilization methods involve distinct trade-off between these effects, thus emphasizing the need for a holistic (systems) view of immobilized enzymes for the rational development of practical biocatalysts.
Original language | English |
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Article number | 140333 |
Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
Volume | 1868 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1 Feb 2020 |
Keywords
- Biocatalyst
- Enzyme
- Immobilization
- Single-molecule analysis
- Solid-liquid interface
ASJC Scopus subject areas
- Analytical Chemistry
- Biophysics
- Biochemistry
- Molecular Biology