Event Information
Production of linear cellodextrins and a designer minicellulosome scaffoldin in the progress towards a biophysical description of the cellulosome.
- Abstract:
The cellulosome is a modular, multi-enzyme complex reported to hydrolyze recalcitrant lignocellulosic biomass with synergistic improvement over free cellulase systems. Thus, it has become an interesting target of study in both renewable energy technology and enzymology communities. In this report, current and future efforts to explore the nature of the apparent synergy within the cellulosome system using a combination of biophysical enzymology and organic chemistry are discussed. To this end, a recombinant cellulosome scaffoldin has been expressed from Escherichia coli, and linear, water-soluble cellodextrins have been synthesized via a mild pivaloylysis of cellulose triacetate. Potential methods in which designer mini-cellulosomes and cellodextrins are to be used to quantify the solution phase thermodynamics and kinetics of cellulolysis are described. Specifically, isothermal titration calorimetry (ITC) will be used to quantify cellulosome-substrate association, and liquid chromatography – mass spectrometry (LCMS) will be used to quantify cellulase activity on soluble substrates. Finally, methods to extrapolate these solution phase observations into a characterization of the carbohydrate binding and hydrolytic activity of the cellulosome on insoluble and complex substrates are outlined.
Preliminary Examination Seminar
Student Exams Seminar