Growth and expression of relevant metabolic genes of Clostridium thermocellum cultured on lignocellulosic residues

Author:

Leitão Vanessa O1,Noronha Eliane F1,Camargo Brenda R1,Hamann Pedro R V1,Steindorff Andrei S1,Quirino Betania F2,de Sousa Marcelo Valle3,Ulhoa Cirano J4,Felix Carlos R1

Affiliation:

1. 0000 0001 2238 5157 grid.7632.0 Laboratory of Enzymology, Department of Cell Biology University of Brasília (UnB) 70910-900 Brasília DF Brazil

2. Embrapa-Agroenergy Brasília DF Brazil

3. 0000 0001 2238 5157 grid.7632.0 Laboratory of Biochemistry and Chemistry of Proteins, Department of Cell Biology University of Brasília (UnB) Brasília DF Brazil

4. grid.411195.9 0000 0001 2192 5801 Laboratory of Enzymology, Department of Cell Biology University Federal Goiás Goiania GO Brazil

Abstract

Abstract The plant cell wall is a source of fermentable sugars in second-generation bioethanol production. However, cellulosic biomass hydrolysis remains an obstacle to bioethanol production in an efficient and low-cost process. Clostridium thermocellum has been studied as a model organism able to produce enzymatic blends that efficiently degrade lignocellulosic biomass, and also as a fermentative microorganism in a consolidated process for the conversion of lignocellulose to bioethanol. In this study, a C. thermocellum strain (designated B8) isolated from goat rumen was characterized for its ability to grow on sugarcane straw and cotton waste, and to produce cellulosomes. We also evaluated C. thermocellum gene expression control in the presence of complex lignocellulosic biomasses. This isolate is capable of growing in the presence of microcrystalline cellulose, sugarcane straw and cotton waste as carbon sources, producing free enzymes and residual substrate-bound proteins (RSBP). The highest growth rate and cellulase/xylanase production were detected at pH 7.0 and 60 °C, after 48 h. Moreover, this strain showed different expression levels of transcripts encoding cellulosomal proteins and proteins with a role in fermentation and catabolic repression.

Funder

Universidade de Brasília

CNPq

CAPES

FAPDF

Embrapa

FINEP

Publisher

Oxford University Press (OUP)

Subject

Applied Microbiology and Biotechnology,Biotechnology,Bioengineering

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