Thermostabilization of DNA Polymerase with Novel Chaperones

OverviewDr. 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 e…

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.