Peroxicats [peroxidases as biocatalysts]. Novel and more robust fungal peroxidases as industrial biocatalysts.
Seventh Framework Programme. Food, Agriculture and Fisheries, and Biotechnology (KBBE). Grant agreement nº: KBBE-2010-4-265397. Total budget: 4.3 million €; EC-funding: 3 million €.
Enzymes catalyzing redox reactions (oxidoreductases) represent an environmentally friendly alternative to harsh chemicals in industrial processes that include oxidative transformations for production of chemicals and other value-added products with large markets in developed and emerging economies.
Fungi and other
microorganisms provide the wider and more easily
exploitable source for oxidative enzymes.
However, the
penetration of microbial oxidoreductases in the chemical markets is
still low despite the
recent discovery of very
promising enzymes.
The use of these enzymes as biocatalysts requires
tuning their
catalytic and
operational properties (a type of manipulation that is possible nowadays using protein engineering tools).
Overview of reactions catalyzed by heme-thiolate peroxidases (HTP).
In addition to microbial screening, the huge amount of
genomic resources available nowadays, and to be generated during the course of the project, will be
exploited in the search for new fungal peroxidase/peroxygenases.
Automatic extraction system.
Some of the main issues presently limiting the industrial application of peroxidases will be addressed, such as:
Their suicide
inactivation by H
2O
2
Low functional
expression
Limited
oxygen transfer potential
Moreover, the
catalytic properties of the most interesting enzymes will be
modulated to adapt them to the industrial processes.
A combination of
rational and
non-rational design will be used, based on directed mutagenesis, and random mutagenesis (together with high-throughput screening), respectively.
The reaction mechanisms and industrial interest of the selected peroxidases/ peroxygenases will be studied using
modern analytical techniques, including two-dimensional NMR, that are able to provide information on the modifications produced on both simple and complex substrates.
In this way novel and robust peroxidases/peroxygenases will be obtained with high potential both in
bulk chemistry, e.g. for hydrocarbon
oxyfunctionalization and
oxidation of recalcitrant compounds, and
fine chemistry, e.g. substituting costly hydroxylation reactions in the pharmaceutical sector.