Synergistic enzymatic and microbial lignin conversion
- Texas A & M Univ., College Station, TX (United States)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Georgia Inst. of Technology, Atlanta, GA (United States)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
- Texas A & M Univ., College Station, TX (United States); Cleamol LLC, College Station, TX (United States)
We represent the utilization of lignin for fungible fuels and chemicals and it's one of the most imminent challenges in modern biorefineries. However, bioconversion of lignin is highly challenging due to its recalcitrant nature as a phenolic heteropolymer. This study addressed the challenges by revealing the chemical and biological mechanisms for synergistic lignin degradation by a bacterial and enzymatic system, which significantly improved lignin consumption, cell growth and lipid yield. The Rhodococcus opacus cell growth increased exponentially in response to the level of laccase treatment, indicating the synergy between laccase and bacterial cells in lignin degradation. Other treatments like iron and hydrogen peroxide showed limited impact on cell growth. Chemical analysis of lignin under various treatments further confirmed the synergy between laccase and cells at the chemical level. 31P nuclear magnetic resonance (NMR) suggested that laccase, R. opacus cell and Fenton reaction reagents promoted the degradation of different types of lignin functional groups, elucidating the chemical basis for the synergistic effects. 31P NMR further revealed that laccase treatment had the most significant impact for degrading the abundant chemical groups. The results were further confirmed by the molecular weight analysis and lignin quantification by the Prussian blue assay. The cell–laccase fermentation led to a 17-fold increase of lipid production. Overall, the study indicated that laccase and R. opacus can synergize to degrade lignin efficiently, likely through rapid utilization of monomers generated by laccase to promote the reaction toward depolymerization. The study provided a potential path for more efficient lignin conversion and development of consolidated lignin conversion.
- Research Organization:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- USDOE Office of Energy Efficiency and Renewable Energy (EERE)
- Grant/Contract Number:
- AC05-00OR22725; EE0006112
- OSTI ID:
- 1265874
- Alternate ID(s):
- OSTI ID: 1376572
- Journal Information:
- Green Chemistry, Journal Name: Green Chemistry Journal Issue: 5 Vol. 18; ISSN GRCHFJ; ISSN 1463-9262
- Publisher:
- Royal Society of ChemistryCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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