Exoproteomics Reveals Outer Membrane Vesicle Mediated Catabolism of Lignin-Derived Aromatics by P. putida KT2440
Lignin is an abundant component of plant cell walls which is heterogeneous and highly resistant to degradation. Biological funneling of lignin via microbes represents an efficient approach for reducing chemical heterogeneity and generating molecules which can be valorized into performance-advantaged materials. Pseudomonas putida KT2440 (P. putida) catabolizes lignin-derived aromatic monomers rapidly and efficiently via the b-ketoadipate (bKA) pathway and our data suggest P. putida may depolymerize HMW lignin as well [1]. The mechanism by which HMW lignin is depolymerized by bacteria remains unknown. Intriguingly, we found that P. putida secretes outer membrane vesicles (OMVs) of two distinct sizes in the presence of lignin. Here, we describe the temporal proteome of OMVs and the vesicle-free secretome (VFS) in the presence or absence of lignin. Enzymes involved in aromatic catabolism via the bKA pathway are temporally enriched into OMVs in the presence of lignin. Isolated OMVs enhance growth of P. putida mutants unable to grow on model lignin-derived aromatics, and turnover protocatechuic acid in vitro. Together, this work leads us to hypothesize mechanisms by which OMVs contribute to extracellular aromatic catabolism by P. putida. Ongoing and future work seeks to further understand this phenomena in the context of both fundamental an applied lignin conversion research areas.
- Research Organization:
- National Renewable Energy Lab. (NREL), Golden, CO (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- DOE Contract Number:
- AC36-08GO28308
- OSTI ID:
- 1606131
- Report Number(s):
- NREL/PO-5100-74567
- Resource Relation:
- Conference: Presented at the 17th International Conference on Pseudomonas, 22-26 July 2019, Kuala Lumpur, Malaysia
- Country of Publication:
- United States
- Language:
- English
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