Predicting enzyme adsorption to lignin films by calculating enzyme surface hydrophobicity [Protein Structure and Folding]

May 29th, 2014 by Sammond, D. W., Yarbrough, J. M., Mansfield, E., Bomble, Y. J.., Hobdey, S. E., Decker, S. R., Taylor, L. E., Resch, M. G., Bozell, J. J., Himmel, M. E., Vinzant, T. B., Crowley, M. F.

The inhibitory action of lignin on cellulase cocktails is a major challenge to the biological saccharification of plant cell wall polysaccharides. While 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.