TECHNOLOGYThermostabilization of DNA Polymerase with Novel Chaperones
Overview
Dr. Frank Robb has considerable expertise in the study of microbes found in extreme environments and their mechanisms of survival. These astonishing organisms have protein chaperone systems that enable them to survive and even thrive in extreme heat and harsh chemical conditions. An important application for these chaperones is to enhance protein folding and increase enzyme or microbial resistance to heat. The hyperthermophilic organism Pyrococcus furiosus grows optimally at 100 degrees C. Dr. Robb found that the thermo-stability of Taq polymerase was significantly improved by combinations of P. furiosus chaperones, showing ongoing protein folding activity at elevated temperatures and during thermal cycling. These properties may be exploited to enhance the durability and cost effectiveness of high temperature biocatalysts.(FR-2010-087; & FR-2010-089)
Applications
Enhance protein expression and stability in high-temperature systems.
Advantages
Novel composition & method to protect enzyme activity, in particular DNA polymerase.
Stage of Development
Well characterized as research tool with industrial applications.
R&D Required
Adaptation to a specific product.
Licensing Potential
UMB is seeking partners to develop and commercialize multiple applications of this technology.
Contact Info
Office of Technology Transfer
620 W Lexington St., 4th Floor
Baltimore, MD 21201
Email: [email protected]
Phone: (410) 706-2380
