Abstract: 

The alcohol dehydrogenase D from Pyrococcus furiosus is a thermostable oxidoreductase enzyme with broad substrate specificity.  We have engineered just about every facet of its enzymatic activity including its cofactor specificity and substrate specificity.  We have engineered it to use a non-native cofactor, which improves biofuel cell performance.  We have introduced a calcium-binding peptide, enabling cofactor selectivity to be dynamically tuned.  We have used super-charged proteins to alter the catalytic microenvironment without active site mutagenesis.  And we have used directed evolution to eliminate the catalytic activity of the enzyme and convert it into an explosive-binding protein for biosensor applications.  Finally, we have developed new theory-based figures of merit for comparing the performance of bi-reactant and other multi-reactant enzymatic mechanisms.

Bio: 

Scott Banta is Professor and Chair of Chemical Engineering at Columbia University.  He received his B.S.E. degree from the University of Maryland, Baltimore County, and his M.S. and Ph.D. degrees from Rutgers University.  He did a postdoctoral fellowship at the Shriners and Massachusetts General Hospitals and Harvard Medical School.  He began his faculty career in the Department of Chemical Engineering at Columbia University in 2004 and his research has focused on the engineering of proteins and peptides for various applications in areas including biocatalysis, bioelectrocatalysis, biomaterials, gene and drug delivery, biosensing, and bioenergy. His group is also developing new biotechnology platforms for energy harvesting and conversion as well as metal and mineral processing.