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J Biol Chem. 2014 Jul 25;289(30):20960-9. doi: 10.1074/jbc.M114.573642. Epub 2014 May 29.

Predicting enzyme adsorption to lignin films by calculating enzyme surface hydrophobicity.

Author information

1
From the Biosciences Center and.
2
the Applied Chemicals and Materials Division, National Institute for Standards and Technology, Boulder, Colorado 80305, and.
3
From the Biosciences Center and National Bioenergy Center, National Renewable Energy Laboratory, Golden, Colorado 80401.
4
the Center for Renewable Carbon, Center for the Catalytic Conversion of Biomass (C3Bio), University of Tennessee, Knoxville, Tennessee 37917.
5
From the Biosciences Center and Michael.Crowley@nrel.gov.

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.

KEYWORDS:

Cellulase; Enzyme Inhibitor; Glycoside Hydrolase; Hydrophobic Interaction; Lignin; Protein Chemistry; Protein Engineering

PMID:
24876380
PMCID:
PMC4110302
DOI:
10.1074/jbc.M114.573642
[Indexed for MEDLINE]
Free PMC Article
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