Predicting Enzyme Adsorption to Lignin Films by Calculating Enzyme Surface Hydrophobicity

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D. W. Sammond, J. M. Yarbrough, E. Mansfield, Y. J. Bomble, S. E. Hobdey, S. R. Decker, L. E. Taylor, M. G. Resch, J. J. Bozell, M. E. Himmel, T. B. Vinzant, and M. F. Crowley, “Predicting Enzyme Adsorption to Lignin Films by Calculating Enzyme Surface Hydrophobicity,” Journal of Biological Chemistry, vol. 289, no. 30, pp. 20960–20969, Jul. 2014.

Type Journal Article
Author Deanne W. Sammond
Author John M. Yarbrough
Author Elisabeth Mansfield
Author Yannick J. Bomble
Author Sarah E. Hobdey
Author Stephen R. Decker
Author Larry E. Taylor
Author Michael G. Resch
Author Joseph J. Bozell
Author Michael E. Himmel
Author Todd B. Vinzant
Author Michael F. Crowley
Volume 289
Issue 30
Pages 20960-20969
Publication Journal of Biological Chemistry
Date July 25, 2014
Journal Abbr Journal of Biological Chemistry
Abstract The inhibitory action of lignin on cellulase cocktails is a major challenge to the biological saccharification of plant cell wall polysaccharides. Although the mechanism remains unclear, hydrophobic interactions between enzymes and lignin are hypothesized to drive adsorption. Here we evaluate the role of hydrophobic interactions in enzyme-lignin binding. The hydrophobicity of the enzyme surface was quantified using an estimation of the clustering of nonpolar atoms, identifying potential interaction sites. The adsorption of enzymes to lignin surfaces, measured using the quartz crystal microbalance, correlates to the hydrophobic cluster scores. Further, these results suggest a minimum hydrophobic cluster size for a protein to preferentially adsorb to lignin. The impact of electrostatic contribution was ruled out by comparing the isoelectric point (pI) values to the adsorption of proteins to lignin surfaces. These results demonstrate the ability to predict enzyme-lignin adsorption and could potentially be used to design improved cellulase cocktails, thus lowering the overall cost of biofuel production.



  • Adsorption
  • Cellulase
  • Chemicophysical properties
  • Enzymatic hydrolysis
  • Enzymes
  • Hydrolysis
  • Isoelectric point
  • Proteins
  • Surface area

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