High-capacity and Cost-effective Manufacture of Chloroperoxidase

Period of Performance: 12/21/2012 - 12/17/2013


Phase 2 STTR

Recipient Firm

Agave Biosystems, Inc.
P.O. Box 100
Ithaca, NY 14850
Principal Investigator
Firm POC

Research Institution

Cornell University
426 Phillips Hall
Ithaca, NY 14853
Institution POC


The chloroperoxidase enzyme from the filamentous fungus Caldariomyces fumago has applications in industrial chemical synthesis and the detection and inactivation of chemical warfare agents. Chloroperoxidase is capable of regio- and enantioselective oxygenations and halogenations of organic substrates. When performed chemically, these reactions typically require aggressive reagents and reaction conditions, and lead to the formation of undesired by-products. Widespread adoption of enzyme-catalyzed synthetic strategies is hindered by the high cost of purified proteins, and by the challenges of retaining the native activity of proteins expressed using heterologous host systems. In the Phase I, Agave BioSystems and collaborators from Cornell University achieved high level production of highly active recombinant Caldariomyces fumago chloroperoxidase (rCPO) in Aspergillus. The current not fully optimized levels of expression are five-fold higher than previously reported. They are also 100 fold lower than potential levels which have been achieved with other Aspergillus systems providing enormous upside potential that will be realized upon completion of the Phase II tasks. The result will be an expression system that meets or exceeds the sponsor s specifications.