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
The use of these enzymes as biocatalysts requires tuning
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
Low functional expression
Limited oxygen transfer
Moreover, the catalytic properties
of the most interesting enzymes will be modulated
to adapt them to the industrial processes.
A combination of 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
of recalcitrant compounds, and fine chemistry
, e.g. substituting costly hydroxylation reactions in the pharmaceutical sector.