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Forest Products Laboratory
One Gifford Pinchot Drive
Madison, WI 53726-2398
Phone: (608) 231-9200
Fax: (608) 231-9592


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Institute for Microbial and Biochemical Techology

Project Title :  Enzymatic and microbial processing of wood and wood fiber to fuels and other chemicals
Project Number : FPL-4712-3A
Start Date : 07-23-2007
End Date : 07-22-2012

View the 6 publications associated with this project.

Principal Investigator:
Barbara L. Illman

Non Technical Summary
This research develops basic information and operating conditions needed for efficient and effective enzymatic and microbial processing of wood and wood fiber. Use of this technology enables more efficient use of our forest resources.

Objectives Summary
The objectives of this research are to identify, discover, or create enzymes for the treatment of wood and pulp fibers. For example, the pulp and paper industry uses xylanases to reduce the need for harsh oxidizing chemicals for pulp bleaching. Xylanase prebleaching decreases pollution and provides for more efficient use of chemicals. However existing xylanases are not ideally suited to the equipment and process in which they are used. Research to obtain xylanases that will work under more extreme conditions could broaden the applicability of this environmentally benign technology. In another application, cellulases have been developed for removing inks and contaminants from recycled fibers. Use of this technology enables more efficient use of our forest resources. The technology is not fully robust, so it is not as widely applied as it might be. Further research into enzyme mechanisms or processes could expand the use of recycled fibers and conserve timber while providing the public with material goods. Other possible applications include the use of laccases to modify fiber surfaces and properties and cellulases or cellulose binding domains to modify fiber properties.

Approach Summary
This research will consist of basic and applied studies on the discovery and use of microorganisms and enzymes to treat virgin fibers, recycled fibers, and wood residues. Enzymes possessing the capacity to release lignin and chromophores from pulps will be sought, along with enzymes that might increase the strength of paper made from lower grade residuals and pulp. Enzymes will be purified and characterized, and cloned where it is deemed appropriate to better understand fundamental enzymatic mechanisms or to produce the enzyme in sufficient quantity for further characterization and study. Kinetic constants of the enzymes will be measured, and their modes of action will be assessed. The substrate range of some enzymes will be explored so that better predictions can be made of their effects on wood and wood fibers. The modification of wood and fiber surfaces provides great potential in developing new products. Specific removal or modification of components of the wood may be useful in producing new products some of which may be useful as chemicals or fuels, others as heavy metal or nutrient adsorbants and others having chemicals replaced by enzymatic action. Planned accomplishments include the following 1. Identify novel enzymes, reactants and proteins that help to separate wood components and test if they will provide benefits to processing wood. 2. Improve fundamental understanding of how enzymes might be used to modify wood and fiber surfaces to attach various chemically defined functional groups. 3. Clone and express enzymes of potential interest to study them more easily and better understand their fundamental structural properties. 4. Create novel enzymes that combine a catalytic function with a sequence for immobilization on lignocellulosic residues. 5. Communicate the findings in high-quality scientific papers in refereed journals, in lectures before a variety of audiences, and, where appropriate, in patents that will enhance technology transfer.

Publications associated with this Project

Publication YearTitleDate Posted
2012Complete genome sequence of Paenibacillus sp. strain JDR-209/27/12
2010Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups11/16/11
2009Gene cloning and herologous expression of pyranose 2-oxidase from the brown-rot fungus, Gloeophyllum trabeum02/09/10
2011Ligand bound structures of a glycosyl hydrolase family 30 glucuronoxylan xylanohydrolase09/30/11
2011Pseudomonas sax Genes Overcome Aliphatic Isothiocyanate - Mediated Non-Host Resistance in Arabidopsis11/25/11
2009Pyranose 2-oxidase from Phanerochaete chrysosporium-Expression in E. coli and biochemical characterization02/09/10

Project Summaries last modified: 06-20-2011