Journal
TRENDS IN BIOTECHNOLOGY
Volume 31, Issue 6, Pages 335-341Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibtech.2013.04.002
Keywords
laccases; in vivo metabolism; oxidative coupling; laccase-mediator system
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Funding
- National Research Foundation of Korea (NRF)
- Korea government (MEST) [2012-0008787]
- 'The GAIA Project' by Korea Ministry of Environment
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Laccases have been widely used in several biotechnological areas, including organic synthesis, bioremediation, and pulp/textile bleaching. In most applications, the enzymatic actions start with single-electron oxidation of small organics followed by formation of the corresponding radicals. These radicals are subsequently involved in either oxidative coupling (i.e., bond formation) or bond cleavage of target organics. These bifunctional actions catabolic versus anabolic are readily identifiable in in vivo metabolic processes involving laccases. Here, we characterize the bifunctionality of laccase-mediated oxidation of small organics and present the view that knowledge of the biological functions of these metabolic processes in vivo can illuminate potential biotechnological applications of this bifunctionality.
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