quarta-feira, 2 de junho de 2010

Review - Lacases

Trends Biotechnol. 2010 Feb;28(2):63-72

Designer laccases: a vogue for high-potential fungal enzymes?

Rodgers CJ, Blanford CF, Giddens SR, Skamnioti P, Armstrong FA, Gurr SJ.

Department of Chemistry, South Parks Road, University of Oxford, Oxford OX13QR, UK.

Abstract
Laccases are blue multicopper oxidases that catalyse the four-electron reduction of O(2) to water coupled with the oxidation of small organic substrates. Secreted basidiomycete white-rot fungal laccases orchestrate this with high thermodynamic efficiency, making these enzymes excellent candidates for exploitation as industrial oxidants. However, these fungi are less tractable genetically than the ascomycetes, which predominantly produce lower-potential laccases. We address the state-of-play regarding expression of high reduction potential laccases in heterologous hosts, and issues regarding enzyme glycosylation status. We describe the synergistic role of structural biology, particularly in unmasking structure-function relationships following genetic modification and their collective impact on laccase yields. Such recent research draws closer the prospect of industrial quantities of designer, fit-for-purpose laccases. 2009 Elsevier Ltd.
Link para download:
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6TCW-4XVPFR0-1-8&_cdi=5181&_user=687355&_pii=S0167779909002145&_orig=search&_coverDate=02%2F28%2F2010&_sk=999719997&view=c&wchp=dGLbVzb-zSkWA&md5=626c329397f0fbd1c1a8fe131bd6be20&ie=/sdarticle.pdf

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