Exploring unique compounds from lignin degradation using MnSOD an | 7524
Current Synthetic and Systems Biology

Current Synthetic and Systems Biology
Open Access

ISSN: 2332-0737

Exploring unique compounds from lignin degradation using MnSOD and Dyp-type peroxidase enzymes

2nd International Conference on Systems & Synthetic Biology

August 18-20, 2016 London, UK

Sharon Mendel Williams

Coventry University, UK

Scientific Tracks Abstracts: Curr Synthetic Sys Biol

Abstract :

Lignin is an organic polymer found in the cell walls of plants. Lignin can be used to create biofuels, or as an organic hydrocarbon source for a large variety of chemicals and polymers. However, lignin is very robust and current industrial processes for using it are inefficient. Therefore, a useable biological process for degrading lignin would be of great benefit. Understanding the pathway of lignin degradation, and the byproducts, is essential in order to be able to exploit the use of micro-organisms. Furthermore, we can characterize novel bio-products obtained by enzymatic oxidation of lignin, which could have very interesting applications for industrial biotechnology. In the current project Dyp-type peroxidases from Gram-negative Pseudomonas fluorescens Pf-5 and recombinant Sphingobacterium MnSOD1 and MnSOD2 cloned into E. coli and were investigated. These are bacterial enzymes that are already known to degrade lignin. Different genetic mutations were introduced, and the resulting enzymes were characterized by using them with different lignin substrates. The reaction compounds were analysed by reverse phase HPLC/ GC-MS. The goal is to improve the effectiveness of the enzymes, increase the production of the enzymesand degrade the lignin into different and more useable compounds. Any of these goals would be of valuable scientific and commercial benefit.

Biography :

Sharon Mendel Williams joined Coventry University as a Lecturer in the School of Life Sciences in November 2014. She worked as a Post-doctorate Research Fellow in both Chemistry and Biology departments of Warwick University for 8 years. Her research focuses on the biophysics and biochemistry of proteins, and understanding the mechanisms of enzymes. She has a wide range of depth and experience in molecular biology, biochemistry, and chemistry. She is a member of the Royal Society of Chemistry and has been awarded a grant from the RSC research fund to accomplish the current research.