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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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Protein Structure and Biochemical Characterization of a Novel Functioning Xylanase

The structure model of the new glycoside hydrolase family 30-8 (GH30-8) xylanase (green) overlaid with the previously determined protein structure of a canonical GH30-8 xylanase (blue) indicating that although the new xylanase is functionally unique, it does not structurally differ from the canonical GH30-8 xylanases (top). An alignment showing the specific region of primary amino acid sequence containing the altered sequence (red boxes) attributed to the observed difference in mode of action of this new enzyme against its xylan substrate. USDA Forest Service
The structure model of the new glycoside hydrolase family 30-8 (GH30-8) xylanase (green) overlaid with the previously determined protein structure of a canonical GH30-8 xylanase (blue) indicating that although the new xylanase is functionally unique, it does not structurally differ from the canonical GH30-8 xylanases (top). An alignment showing the specific region of primary amino acid sequence containing the altered sequence (red boxes) attributed to the observed difference in mode of action of this new enzyme against its xylan substrate. USDA Forest Service
Snapshot: Scientists identified and characterized a xylanase with unique function that may have applications in processing of woody biomass substrate.
Summary:

There is strong interest in the discovery of new proteins and enzymes for the processing of woody biomass materials. Xylan is the second most abundant polymeric sugar in hardwoods and grasses. The enzymes which work to degrade these, xylanases, are classified in only a few generally conserved protein families. Those classified as glycoside hydrolase family 30-8 are known to have a unique ability to recognize a specific location along the xylan chain where it then will hydrolyze the polysaccharide. In this work, Forest Service scientists and their research partners have used primary amino acid sequence studies to identify a new GH30-8 xylanase with a unique mode of action toward xylan. Biochemical and protein structure determination provide insight into its unusual function. This enzyme may find application in the processing of woody biomass materials.		Princpal Investigator(s):
 St. Johns, Franz
 Crooks, M.E. Casey


Research Location:
  • Forest Products Laboratory
  • Stanford Synchrotron Radiation Lightsource
  • University of Maryland, Baltimore


Forest Service Partners:
  • Diane Dietrich


External Partners:
  • Edwin Pozharski
  • Elizabeth Bales
  • Jason C. Hurlbert
  • Javier M. Gonzalez
  • Kennon Smith

Fiscal Year: 2015
Highlight ID: 613
 
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