Oxford Biotrans has exclusive access to:

  • An extensive library of novel, custom-designed cytochrome P450 enzymes that have high selectivity for specific substrates and yield products with high efficiency.
  • two master patent families, including granted patents, covering variants of the P450 enzyme P450BM3 and processes to oxidise organic molecules.

The cytochrome P450 monooxygenases are a super-family of heme-dependent enzymes that catalyse the activation of carbon-hydrogen bonds via the insertion of an oxygen atom from atmospheric oxygen. Both activated and non-activated carbon-hydrogen bonds in an extremely diverse range of organic molecules are oxidised by P450 enzymes, in many cases with product selectivity. The oxidation activity of P450 enzymes has no analogues in classical chemical synthesis methodologies, and opens up novel routes for producing chemical compounds, whether drugs or industrial fine chemicals, that are more direct and efficient, often starting from natural, sustainable sources under mild conditions.

Development of processes based on P450 enzyme activity requires the understanding and ultimately control over how the target substrate is bound within the enzyme to achieve high turnover activity and product selectivity (the key parameters that dictate the efficiency of any new process deploying these enzymes). The research team in the Chemistry Department at the University of Oxford has over 15 years experience in the design and evolution of highly active and highly selective P450 enzymes. The existing enzyme library has been developed for the oxidation of linear and cyclic alkanes and alkenes, aromatic compounds, and terpenoid hydrocarbons to a broad range of alcohol and ketone products, which are covered by the patents.