METAPROMIS

New enzymes by identification from metagenomic libraries and directed evolution using microfluidic microdroplets

Coordinatore	THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE    more  Organization address address: The Old Schools, Trinity Lane city: CAMBRIDGE postcode: CB2 1TN contact info Titolo: Mr. Nome: Keith Cognome: Cann Email: send email Telefono: 0044 1223 333 543 Fax: 0044 1223 332 988
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	180˙603 €
EC contributo	180˙603 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2009-IEF
Funding Scheme	MC-IEF
Anno di inizio	2010
Periodo (anno-mese-giorno)	2010-06-01   -   2012-05-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE  Organization address address: The Old Schools, Trinity Lane city: CAMBRIDGE postcode: CB2 1TN contact info Titolo: Mr. Nome: Keith Cognome: Cann Email: send email Telefono: 0044 1223 333 543 Fax: 0044 1223 332 988	UK (CAMBRIDGE)	coordinator	180˙603.20

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 Obiettivo del progetto (Objective)

'The usage of Nature’s catalysts for industrial applications is promising to be one of the central pillars of sustainable European chemistry, due to the reduced environmental impact of ‘green’ biocatalytic processes compared to current hazardous chemical procedures. However, at present a large fraction of chemical transformations cannot be substituted with biotechnological production lines, because suitable biocatalysts satisfying the criteria are not known. Our incomplete understanding of enzyme mechanisms makes it difficult to generate catalysts de novo with protein design techniques. An alternative route is the identification of biocatalysts from the natural collections of evolved proteins that fit into the catalytic task to some extent (a phenomenon known as catalytic promiscuity) and improve their catalytic performance for the desired reaction by directed protein evolution techniques. In order to reach this strategic goal, we aim to employ a new high throughput technology (in vitro compartmentalization in microfluidic water-in-oil emulsion droplets) in the search for new biocatalysts. By this assay technology, previously inaccessibly large enzyme libraries will be screened. After isolation of the target enzymes from microbial metagenomes, the latest protein evolutionary theories in relation to catalytic promiscuity will be investigated on a large set of natural enzyme variants, in order to elucidate how new activities are evolved in nature. The resulting aspects of evolution of new enzyme functions could provide an intellectual framework to rationalise evolutionary developments and to utilize these principles for evolution in the test tube for relevant applications.'