Projects per year
Abstract
Water molecules play a number of critical roles in enzyme catalysis, including mass transfer of substrates and products, nucleophilicity and proton transfer at the active site, and solvent shell-mediated dynamics for accessing catalytically competent conformations. The pervasiveness of water in enzymolysis therefore raises the question concerning whether biocatalysis can be undertaken in the absence of a protein hydration shell. Lipase-mediated catalysis has been undertaken with reagent-based solvents and lyophilized powders, but there are no examples of molecularly dispersed enzymes that catalyse reactions at sub-solvation levels within solvent-free melts. Here we describe the synthesis, properties and enzyme activity of self-contained reactive biofluids based on solvent-free melts of lipase-polymer surfactant nanoconjugates. Desiccated substrates in liquid (p-nitrophenyl butyrate) or solid (p-nitrophenyl palmitate) form can be mixed or solubilized, respectively, into the enzyme biofluids, and hydrolysed in the solvent-free state. Significantly, the efficiency of product formation increases as the temperature is raised to 150 °C.
Original language | English |
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Article number | 5058 |
Number of pages | 8 |
Journal | Nature Communications |
Volume | 5 |
DOIs | |
Publication status | Published - 6 Oct 2014 |
Keywords
- ORGANIC-SOLVENTS
- CATALYZED TRANSESTERIFICATION
- MEDIA
- BIOCATALYSIS
- BIODIESEL
- WATER
- ACID
- ACTIVATION
- STABILITY
- MYOGLOBIN
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Projects
- 2 Finished
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Molten Proteins: synthesis and design of novel biomolecule-based liquid nanomaterials and their application in bionanochemistry
29/08/11 → 29/08/14
Project: Research
Profiles
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Professor Stephen Mann
- The Bristol Centre for Nanoscience and Quantum Information
- Soft Matter, Colloids and Materials
- Biological and Archaeological Chemistry
- School of Chemistry - Professor of Chemistry
Person: Academic , Member
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Professor Adam W Perriman
- School of Cellular and Molecular Medicine - Professor of Bioengineering
- Fundamental Bioscience
Person: Academic , Member