Sunday, May 4, 2008
4-46

Heterologous expression, purification, and characterization of a new phosphorylase from Clostridium thermocellum

Xinhao Ye, Biological Systems Engineering Department, Virginia Tech University, Latham Hall 411, Blacksburg, VA 24061 and Y.-H. Percival Zhang, Biological Systems Engineering Department, Institute for Critical Technology and Applied Science (ICTAS), Virginia Tech University, 210-A Seitz Hall, Blacksburg, VA 24061.

A new phosphorylase gene from Clostridium thermocellum was expressed heterologously in Escherichia coli and purified by a new cellulose-binding-module and regenerated amorphous cellulose purification system.  The biochemical characteristics of this phosphorylase will be presented first.  The preliminary results suggest that this new enzyme has some substrate promiscuity on cellulose. The potential application of this new enzyme is to produce high-yield hydrogen (12 H2 per glucose unit) from amorphous cellulose and water by using the novel synthetic enzymatic pathway containing up to 15 enzymes. This enzyme will be responsible for the first step, the most important step, generation of glucose-1-phosphate from cellulose and phosphate directly. It is expected that a significant fraction of hydrogen could be produced through cellulosic materials through the in vitro synthetic biology technology. 


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