High-capacity and Cost-effective Manufacture of Chloroperoxidase

Award Information
Agency:
Department of Defense
Branch
Army
Amount:
$100,000.00
Award Year:
2011
Program:
STTR
Phase:
Phase I
Contract:
W911NF-11-C-0231
Award Id:
n/a
Agency Tracking Number:
A11A-014-0164
Solicitation Year:
2011
Solicitation Topic Code:
A11a-T014
Solicitation Number:
2011.A
Small Business Information
Agave BioSystems, Inc. (Currently AGAVE BIOSYSTEMS INC.)
P.O. Box 100, Ithaca, NY, -
Hubzone Owned:
Y
Minority Owned:
Y
Woman Owned:
N
Duns:
022552900
Principal Investigator:
John Ramsey
Staff Scientist
(607) 272-0002
jramsey@agavebio.com
Business Contact:
Noe Salazar
President
(512) 373-8601
nsalazar@agavebio.com
Research Institution:
Cornell University
Linda Brainard
12 Day Hall
Ithaca, NY, 14853-
(607) 255-7123
Nonprofit college or university
Abstract
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. Chloroperoxidase is a heavily glycosylated protein, and only when it is expressed in filamentous fungal hosts such as Aspergillus niger are the post-translational modifications necessary for its activity performed with fidelity. Development of optimized Aspergillus strains and constructs has facilitated heterologous expression of a range of secreted proteins. In this Phase I, Agave BioSystems proposes to develop a system for expression and purification of chloroperoxidase (CPO) from C. fumago using the filamentous fungus Aspergillus niger as host. Fermentation conditions will be optimized for high volume and cost-effective production, and the biochemical properties of the recombinant enzyme will be characterized.

* information listed above is at the time of submission.

Agency Micro-sites


SBA logo

Department of Agriculture logo

Department of Commerce logo

Department of Defense logo

Department of Education logo

Department of Energy logo

Department of Health and Human Services logo

Department of Homeland Security logo

Department of Transportation logo

Enviromental Protection Agency logo

National Aeronautics and Space Administration logo

National Science Foundation logo
US Flag An Official Website of the United States Government