Defining the eco-enzymological role of the fungal strain Coniochaeta sp. 2T2.1 in a tripartite lignocellulolytic microbial consortium

Author:

Jiménez Diego Javier1ORCID,Wang Yanfang2,Chaib de Mares Maryam2,Cortes-Tolalpa Larisa2,Mertens Jeffrey A3,Hector Ronald E3,Lin Junyan4,Johnson Jenifer4,Lipzen Anna4,Barry Kerrie4,Mondo Stephen J45,Grigoriev Igor V46,Nichols Nancy N3,van Elsas Jan Dirk2

Affiliation:

1. Microbiomes and Bioenergy Research Group, Department of Biological Sciences, Universidad de los Andes, Carrera 1 No 18A-12, Bogotá, Colombia

2. Cluster of Microbial Ecology, Groningen Institute for Evolutionary Life Sciences, University of Groningen, Nijenborgh 7 9747AG, Groningen, The Netherlands

3. Bioenergy Research Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, Illinois 61604, USA

4. U.S. Department of Energy Joint Genome Institute, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA

5. Bioagricultural Science and Pest Management Department, Colorado State University, Fort Collins, Colorado 80521, USA

6. Department of Plant and Microbial Biology, University of California Berkeley, Berkeley, California 94720-3102, USA

Abstract

ABSTRACT Coniochaeta species are versatile ascomycetes that have great capacity to deconstruct lignocellulose. Here, we explore the transcriptome of Coniochaeta sp. strain 2T2.1 from wheat straw-driven cultures with the fungus growing alone or as a member of a synthetic microbial consortium with Sphingobacterium multivorum w15 and Citrobacter freundii so4. The differential expression profiles of carbohydrate-active enzymes indicated an onset of (hemi)cellulose degradation by 2T2.1 during the initial 24 hours of incubation. Within the tripartite consortium, 63 transcripts of strain 2T2.1 were differentially expressed at this time point. The presence of the two bacteria significantly upregulated the expression of one galactose oxidase, one GH79-like enzyme, one multidrug transporter, one laccase-like protein (AA1 family) and two bilirubin oxidases, suggesting that inter-kingdom interactions (e.g. amensalism) take place within this microbial consortium. Overexpression of multicopper oxidases indicated that strain 2T2.1 may be involved in lignin depolymerization (a trait of enzymatic synergism), while S. multivorum and C. freundii have the metabolic potential to deconstruct arabinoxylan. Under the conditions applied, 2T2.1 appears to be a better degrader of wheat straw when the two bacteria are absent. This conclusion is supported by the observed suppression of its (hemi)cellulolytic arsenal and lower degradation percentages within the microbial consortium.

Funder

U.S. Department of Energy Joint Genome Institute

U.S. Department of Energy

USDA ARS

FAPA project

Universidad de los Andes

Publisher

Oxford University Press (OUP)

Subject

Applied Microbiology and Biotechnology,Ecology,Microbiology

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