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, Stephen Mann*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

46 Citations (Scopus)
460 Downloads (Pure)

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 languageEnglish
Article number5058
Number of pages8
JournalNature Communications
Volume5
DOIs
Publication statusPublished - 6 Oct 2014

Keywords

  • ORGANIC-SOLVENTS
  • CATALYZED TRANSESTERIFICATION
  • MEDIA
  • BIOCATALYSIS
  • BIODIESEL
  • WATER
  • ACID
  • ACTIVATION
  • STABILITY
  • MYOGLOBIN

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