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Processive and nonprocessive cellulases for biofuel production-lessons from bacterial genomes and structural analysis

Journal

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 93, Issue 2, Pages 497-502

Publisher

SPRINGER
DOI: 10.1007/s00253-011-3701-9

Keywords

Synergism; Processivity; Molecular modeling; Swollenin; Oxidoreductase; Cellobiose dehydrogenase

Funding

  1. BioEnergy Science Center
  2. U.S. Department of Energy (DOE) research center
  3. Office of Biological and Environmental Research in the DOE Office of Science

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Cellulases are key enzymes used in many processes for producing liquid fuels from biomass. Currently there many efforts to reduce the cost of cellulases using both structural approaches to improve the properties of individual cellulases and genomic approaches to identify new cellulases as well as other proteins that increase the activity of cellulases in degrading pretreated biomass materials. Fungal GH-61 proteins are important new enzymes that increase the activity of current commercial cellulases leading to lower total protein loading and thus lower cost. Recent work has greatly increased our knowledge of these novel enzymes that appear to be oxido-reductases that target crystalline cellulose and increase its accessibility to cellulases. They appear to carry out the C1 activity originally proposed by Dr Reese. Cellobiose dehydrogenase appears to interact with GH-61 proteins in this function, providing a role for this puzzling enzyme. Cellulase research is making considerable progress and appears to be poised for even greater advances.

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