Author
Listed:
- Alex P. S. Brogan
(Centre for Organized Matter Chemistry and Centre for Protolife Research, School of Chemistry, University of Bristol)
- Kamendra P. Sharma
(Centre for Organized Matter Chemistry and Centre for Protolife Research, School of Chemistry, University of Bristol)
- Adam W. Perriman
(Centre for Organized Matter Chemistry and Centre for Protolife Research, School of Chemistry, University of Bristol
School of Cellular and Molecular Medicine, University of Bristol)
- Stephen Mann
(Centre for Organized Matter Chemistry and Centre for Protolife Research, School of Chemistry, University of Bristol)
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.
Suggested Citation
Alex P. S. Brogan & Kamendra P. Sharma & Adam W. Perriman & Stephen Mann, 2014.
"Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150 °C,"
Nature Communications, Nature, vol. 5(1), pages 1-8, December.
Handle:
RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6058
DOI: 10.1038/ncomms6058
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