Single molecule spectroscopy-guided design of thermostable industrial enzymes (2012–2015)
Recombinant proteins with modified properties are the backbone of biotechnology. To be useful in industrial
settings, the stability of proteins at higher temperatures typically requires improvement. Thermostability is a property that is difficult to select for in most of the currently available selection systems. Here we propose to use a combination of cell-free protein expression and on-microfluidic chip single molecule analysis to test
thermostability of proteins. A high-throughput version of this tool will be used to develop thermostabilised versions of phytase, xylanase and beta-glucanase. Such enzymes will allow manufacturing of a new generation of functionalised feedstock and improve competitiveness of Australian agriculture.