Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150 °C

Alex P. S. Brogan, Kamendra P. Sharma, Adam W. Perriman () and Stephen Mann ()
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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
Stephen Mann: Centre for Organized Matter Chemistry and Centre for Protolife Research, School of Chemistry, University of Bristol

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6058

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