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High-capacity and Cost-effective Manufacture of Chloroperoxidase

Award Information
Agency: Department of Defense
Branch: Army
Contract: W911NF-13-C-0009
Agency Tracking Number: A2-5085
Amount: $374,999.00
Phase: Phase II
Program: STTR
Solicitation Topic Code: A11a-T014
Solicitation Number: 2011.A
Solicitation Year: 2011
Award Year: 2013
Award Start Date (Proposal Award Date): 2012-12-21
Award End Date (Contract End Date): 2013-12-17
Small Business Information
P.O. Box 100
Ithaca, NY -
United States
DUNS: 022552900
HUBZone Owned: Yes
Woman Owned: No
Socially and Economically Disadvantaged: Yes
Principal Investigator
 John Ramsey
 Staff Scientist
 (607) 272-0002
Business Contact
 Noe Salazar
Title: President
Phone: (512) 656-6200
Research Institution
 Cornell University
 Linda Brainard
12 Day Hall
Ithaca, NY 14853-
United States

 (607) 255-7123
 Nonprofit College or University

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.

* Information listed above is at the time of submission. *

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