Author
Rich, Joseph | |
Anderson, Amber | |
LARSON, T - Augustana College |
Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 9/10/2014 Publication Date: 9/10/2014 Citation: Rich, J.O., Anderson, A.M., Larson, T.M. 2014. Selective oxidation of lignin model compounds – a combinatorial application of the laccase-mediator system [abstract]. European Symposium on Biochemical Engineering Sciences. L-K13. Interpretive Summary: Technical Abstract: Identifying suitable reaction conditions remains an important task in the development of practical enzyme catalysts. 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. While many of the literature reports have described single enzyme-mediator pairs, we will describe a combinatorial approach to the laccase-mediated system (LMS) where 16 enzymes were each paired with 30 different previously reported mediators. We determined the pH optimum (4.4–6.4) and operational temperature range (25–80 °C) for each enzyme. The LMS reaction was optimized to achieve near quantitative yields in the oxidation of veratryl alcohol to veratrylaldehyde. Although each of the mediators had been previously reported to serve as a laccase-mediator, it is clear that for a given substrate, it is necessary to examine a wide variety of enzyme-mediator combinations, and this combinatorial approach will enable the rapid identification of a suitable enzyme-mediator combination and optimization of reaction conditions. The application of the LMS for the modification of lignin model compounds, including novel biobased products from these reactions, will also be discussed. |