TY - JOUR
T1 - Predicting Enzyme Adsorption to Lignin Films by Calculating Enzyme Surface Hydrophobicity
AU - Sammond, Deanne
AU - Yarbrough, John
AU - Bomble, Yannick
AU - Hobdey, Sarah
AU - Decker, Steve
AU - Resch, Michael
AU - Himmel, Michael
AU - Vinzant, Todd
AU - Crowley, Michael
AU - Mansfield, Elisabeth
AU - Bozell, Joseph
AU - Taylor, Larry
PY - 2014/7/25
Y1 - 2014/7/25
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84905398142&partnerID=8YFLogxK
U2 - 10.1074/jbc.M114.573642
DO - 10.1074/jbc.M114.573642
M3 - Article
C2 - 24876380
AN - SCOPUS:84905398142
SN - 0021-9258
VL - 289
SP - 20960
EP - 20969
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 30
ER -