Title: Evaluation of laccase-mediator system (LMS) in the oxidation of veratryl alcohol Authors
Submitted to: Biotechnology Letters
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: October 15, 2012
Publication Date: October 18, 2012
Repository URL: http://link.springer.com/article/10.1007%2Fs10529-012-1078-1
Citation: Larson, T.M., Anderson, A.M., Rich, J.O. 2012. Combinatorial evaluation of laccase-mediator system in the oxidation of veratryl alcohol. Biotechnology Letters. 35(2):225-231. DOI: 10.1007/s10529-012-1078-1. Interpretive Summary: One approach to developing environmentally friendly chemical reactions is the use of enzyme catalysts. Developing reaction systems that are compatible with enzyme activity remains an important challenge. We report a broad range of reaction conditions, including pH, temperature and organic co-solvent, for a laccase-mediated oxidation and is the most comprehensive study to-date of laccase-mediated oxidation of veratryl alcohol. These results will benefit researchers in the development of enzyme catalyzed reactions.
Technical Abstract: Identifying suitable reaction conditions remains an important task in the development of enzyme catalysis. Laccases play an important role in the biological break down of lignin and have great potential in the deconstruction of lignocellulosic feedstocks. We examined 16 laccases, both commercially prepared and crude extracts, for their ability to oxidize veratryl alcohol in the presence of various solvents and mediators. This report provides the most comprehensive study to-date of laccase-mediated oxidation of veratryl alcohol.