In the context of global needs for sustainability and clean manufacturing technologies, biocatalysts are an attractive alternative for the achievement of chemical transformations. Enzymes are non-toxic, biodegradable and efficient/selective biocatalysts with outstanding catalytic properties, offering high levels of safety, low energy consumption and an overall environmentally friendly production procedure. Over 500 commercial products are produced via biocatalysis, which makes the industrial enzyme business important, finding major applications in food-, detergent-, textile-, leather-, pulp- and paper-industries.
Microorganisms are the main source of biocatalysts, with candidates from extreme environments being preferred. Enzymes currently used in industry have been obtained mostly from bacteria and fungi. However, natural occurring enzymes are not optimized to work under industrial or process conditions. In this context, protein engineering has emerged to evolve enzymes in vitro which implicates the generation of mutant libraries, the screening or selection for the best mutants, and the iteration of this process until the desired degree of catalyst improvement has been achieved. Properties such stability, solvent resistance, pH- and temperature-tolerance, efficiency and specificity can be improved by protein engineering strategies. Rational design and directed evolution are the two most general approaches to attempt protein engineering. 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 mutagenesis, meaning that less protein structural knowledge is needed.
In our group we are interested in developing three research lines: 1) Enzyme discovery from Chilean extremophiles, 2) Protein engineering for enzyme specificity and selectivity, and 3) Synthesis of intermediates molecules of industrial interest by biocatalytic processes.