Adaptation of chemical industry to current demand of new products while keeping a profile of low environmental impact is a major challenge. The replacement of complex chemical transformation processes by biological catalysts (biocatalysts) can simplify the process, decrease the amount of chemical solvents used and produce a strong reduction in production costs. The biocatalyst are derived from enzymes, which are proteins produced by living organisms that catalyze the transformation of metabolites and other biological substrates. For their use in the industry, enzymes have to be modified to improve their catalytic properties with the required industrial substrate and to withstand the currently non physiological conditions of industrial use. Modification or discovery of new enzymes suitable for their use as catalysts requires an enormous screening effort, which limits the pace of industrial adaptation. One of the most seek traits in such screenings is thermal stability (), which results in longer use, lesser storage and transportation costs, and functional compatibility with organic solvents.
The HOTDROPS project connects four companies and four academic partners to develop an "Ultra High-throughput platform” for the selection of thermostable proteins, combining Microbiology, Genetics, Biochemistry and Microfluidics. This project will use protein expression systems derived from the thermophilic bacterium Thermus thermophilus in combination with folding reporters that inform indirectly of the of any given protein through the emission of a fluorescent signal. Controlled of the expression system in microdroplets combined with a fluorescence selection microfluidic device will allow for the screening of improbable thermostable enzyme variants among huge numbers of candidates (10e9) in a very short time. Libraries of variants from non-thermostable enzymes and from will be analysed throught the HOTDROPS platform.