Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 15, Issue 45, Pages 9539-9551Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7ob01880k
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Funding
- Army Research Office [W911NF-11-1-0251]
- Defence Threat Reduction Agency [HDTRA-1-11-1-0019, HDTRA-1-16-1-0004]
- National Institutes of Health [GM 093088]
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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.
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