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

J Ind Microbiol Biotechnol. 2017 Jun;44(6):825-834. doi: 10.1007/s10295-017-1915-2. Epub 2017 Feb 8.

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.

Keywords: Agro-industrial residues; Biofuel; Cellulosome; Clostridium thermocellum.

MeSH terms

  • Animals
  • Biomass
  • Cellulase / metabolism
  • Cellulosomes / metabolism
  • Clostridium thermocellum / enzymology*
  • Clostridium thermocellum / genetics
  • Clostridium thermocellum / growth & development
  • Clostridium thermocellum / isolation & purification
  • Fermentation / genetics
  • Gene Expression Regulation, Bacterial
  • Goats
  • Lignin / metabolism*
  • Xylosidases / metabolism

Substances

  • lignocellulose
  • Lignin
  • Xylosidases
  • Cellulase