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Optimization of a Small Laccase by Active‐Site Redesign
Author(s) -
Toscano Miguel D.,
De Maria Leonardo,
Lobedanz Sune,
Østergaard Lars H.
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201300256
Subject(s) - streptomyces coelicolor , laccase , active site , chemistry , mutagenesis , combinatorial chemistry , protein engineering , streptomyces , site directed mutagenesis , redox , directed evolution , small molecule , nanotechnology , biochemical engineering , enzyme , biochemistry , materials science , organic chemistry , biology , mutation , engineering , mutant , genetics , bacteria , gene
Small but faster : A small laccase from Streptomyces coelicolor (SLAC) has been engineered by structure‐based design and site‐directed mutagenesis to improve the activity on commercially relevant substrates. The variants generated showed up to 40‐fold increased efficiency on 2,6‐dimethoxyphenol and the ability to use mediators with considerably higher redox potentials (methylsyringate and TEMPO).