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Biocatalysts can replace harsh chemicals that cause environmental contamination in a variety of industrial processes. Our model enzyme has been the bacterial CotA-laccase from Bacillus subtilis. Following the 3D structure determination, mechanistic and engineering studies are underway aimed at understanding functional and structural determinants of laccase activity and stability. This understanding will allow the design of optimized enzymes that better fit environmental or industrial applications. The research is multidisciplinary, covering:
Search for novel prokaryotic enzymes with potential for industrial applications, Recombinant gene expression, protein production and purification, Spectroscopic and catalytic characterization, Stability characterization, Structural analysis by Molecular Modelling or X-Ray Crystallography with ITQB collaborators, Enzyme engineering by site-directed or random mutagenesis followed by high-throughput screening (directed evolution). Mechanistic studies with substrates of interest (synthetic dyes or lignin based compounds) On a more technological side, we have focused on the biodegradation and biosynthesis of synthetic industrial colorants, namely the important azo and anthraquinonic dyes. From the 106 tons of synthetic dyes produced every year, over 10% is released in wastewaters, as stable organic pollutants. Resorting to biotechnology for the transformation of these dyes is both technically very attractive and quite promising. More recently we have begun investigating the enzymatic bioconversions of lignin, the recalcitrant biopolymer that gives wood its strength. In the carbon cycle, degradation of lignin is a limiting step and clean technologies to unlock lignin, and hence cellulose, as renewable sources of chemicals and fuels may have great importance in the future. |
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Microbial & Enzyme Technology
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INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA |
