Oral Presentation 6-04

 

Effects of Pretreatment on the Activity of Enzymes in Plants:

 Cellulase Enzymes and Ribulose Diphosphate Carboxylase

 

Farzaneh Teymouri and Bruce E. Dale

 

Department of Chemical Engineering and Materials Science

Room 2527, Engineering Building

Michigan State University, East Lansing, MI  48824-1226

 

Telephone:  (517) 353-6777; Fax:  (517) 432-1105; E-mail:  bdale@egr.msu.edu

  

 

A major economic obstacle in bioconverting lignocellulosic materials to ethanol and other products is high cellulase costs.  These costs could conceivably be reduced by genetically transforming plants with cellulase genes to produce the desired enzymes, perhaps even releasing active cellulases from the plants during bioconversion.  Lignocellulose conversion economics might also be enhanced by coproducing valuable proteins in the lignocellulosic biomass.  Under both scenarios, retention of protein activity during processing is a pivotal consideration. 

 

We measured the effects of various lignocellulose pretreatments employing a range of treatment pH values and temperatures on the activity of several plant-produced enzymes.  Enzyme activities and plant materials included transgenic tobacco plants expressing E1 (endoglucanase from Acidothermus cellulolyticus).  The E1 activity was measured in fresh (green) tobacco leaves, in dried leaves and finally in pretreated leaves to characterize the effects of various pretreatments on E1 activity.  Maize transformed with the cellobiohydrolase (CBHI) gene from Trichoderma reesei and the effects of pretreatment on enzyme activity were determined.  Finally, we chose ribulose diphosphate carboxylase (Rubisco) from tobacco and alfalfa plants as a marker to probe the effects of pretreatment on the plants’ own bioactive proteins.  Several pretreatments appear to offer hope for preserving protein activity during processing.

 

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