Single molecule spectroscopy-guided design of thermostable industrial enzymes (2012-2015)
Abstract
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.
