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- Title
An Engineered Laccase from Fomitiporia mediterranea Accelerates Lignocellulose Degradation.
- Authors
Pham, Le Thanh Mai; Deng, Kai; Choudhary, Hemant; Northen, Trent R.; Singer, Steven W.; Adams, Paul D.; Simmons, Blake A.; Sale, Kenneth L.
- Abstract
Laccases from white-rot fungi catalyze lignin depolymerization, a critical first step to upgrading lignin to valuable biodiesel fuels and chemicals. In this study, a wildtype laccase from the basidiomycete Fomitiporia mediterranea (Fom_lac) and a variant engineered to have a carbohydrate-binding module (Fom_CBM) were studied for their ability to catalyze cleavage of β-O-4′ ether and C–C bonds in phenolic and non-phenolic lignin dimers using a nanostructure-initiator mass spectrometry-based assay. Fom_lac and Fom_CBM catalyze β-O-4′ ether and C–C bond breaking, with higher activity under acidic conditions (pH < 6). The potential of Fom_lac and Fom_CBM to enhance saccharification yields from untreated and ionic liquid pretreated pine was also investigated. Adding Fom_CBM to mixtures of cellulases and hemicellulases improved sugar yields by 140% on untreated pine and 32% on cholinium lysinate pretreated pine when compared to the inclusion of Fom_lac to the same mixtures. Adding either Fom_lac or Fom_CBM to mixtures of cellulases and hemicellulases effectively accelerates enzymatic hydrolysis, demonstrating its potential applications for lignocellulose valorization. We postulate that additional increases in sugar yields for the Fom_CBM enzyme mixtures were due to Fom_CBM being brought more proximal to lignin through binding to either cellulose or lignin itself.
- Subjects
LIGNOCELLULOSE; LACCASE; LIGNINS; LIGNIN structure; BIODIESEL fuels; DEPOLYMERIZATION; MIXTURES; IONIC liquids
- Publication
Biomolecules (2218-273X), 2024, Vol 14, Issue 3, p324
- ISSN
2218-273X
- Publication type
Article
- DOI
10.3390/biom14030324