Lignin is a plant cell wall polymer that inhibits enzymatic saccharification of polysaccharides for the production of biofuel. 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. This method could be used to design improved cellulase cocktails to lower the cost of biofuel production.

Enzyme surface hydrophobicity predicts enzyme adsorption to lignin films

249th National Meeting (2015)

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