Utilization of lignocellulosic polysaccharides

Lignocellulosic biomass represents a vast supply of fermentable carbohydrates and functional aromatic compounds. Conversion of lignocellulosics to ethanol and other useful products would be of widespread economical and environmental benefit. Better understanding of the behavior of different lignocellulosic feedstocks in fermentation protocols as well as catalytic activities involved in lignocellulosic depolymerization will further enhance the commercial viability of biomass-to-ethanol conversion processes.;The relative toxicity of the combined non-xylose components in prehydrolysates derived from three different lignocellulosic biomass feedstocks (poplar, corn stover and switchgrass, or Panicum virgatum L.) was determined using a Pichia stipits fermentation assay. The relative toxicity of the prehydrolysates, in decreasing order, was poplar-derived prehydrolysates ;Differences in the relative toxicity of xylose-rich prehydrolysates derived from woody and herbaceous feedstocks are likely due to the relative abundance of a variety of inhibitory compounds, e.g. acetate and aromatic compounds. Fourteen aromatic monomers present in prehydrolysates prepared from corn stover, switchgrass, and poplar were tentatively identified by comparison with published mass spectra. The concentrations of the aromatic monomers totaled 112, 141 and 247 mg(l);The cellulases of Trichoderma reesei are the most widely studied for use in the depolymerization of lignocellulosics. The Trichoderma cellobiohydrolases CBH1 and CBH2 are traditionally categorized as exo-acting cellulases. A simple individual-based model was created to explore the potential effects of native endo activity on substrate-velocity profiles. The model results indicate that an enzyme with a small amount of endo activity will show an apparent substrate inhibition as substrate levels are increased. Actual hydrolysis studies using affinity chromatography-purified CBH2 preparations from three laboratories indicate that CBH2 has native endo activity, while CBH1 does not.