Enzymes are non-toxic, biodegradable and efficient/selective biocatalysts with excellent catalytic properties, offering safety, low energy consumption and an overall environmentally friendly production procedure, which makes them attractive in the context of global needs for sustainability and good manufacturing practice. Based on these considerations, our research interests are centered in the search of novel genes codifying for enzymes of industrial relevance, which might help to avoid the use of hazardous chemical compounds and reduce the accumulation of toxic waste, e.g. produced by traditional (transition)-metal catalysis.
Microorganisms, especially extremophiles, are the main source for the isolation and recombinant expression of novel enzymes. Chile possess a great diversity of extreme environments such as the Atacama Desert, one of the most extreme environments on Earth harboring conditions as dryness and intense solar radiation. In the other end, extreme cold temperatures characterize Chilean Antarctic environments. All along its territory, Chile possesses also several active volcanoes, which may be a source of thermophilic microorganisms. All of these regions have been scarcely explored; therefore microorganisms thriving in those environments are potential sources of novel chemistry.
Since wild-type enzymes are not adapted to an application in industrial conditions, critical properties such as stability, enantio-, stereo- and regioselectivity, solvent-, pH- and temperature-tolerance, overall efficiency and specificity should be optimized by protein engineering. This field evolves enzymes in vitro, using rational design and directed evolution approaches. Rational design is based on site-specific mutagenesis, therefore the structure, function, and catalytic mechanisms of the protein must be known. On the other hand, directed evolution utilizes random or structure-based, focused mutagenesis, meaning that less protein structural knowledge is obligatory.
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