Optimization of synergism of a recombinant auxiliary activity 9 from Chaetomium globosum with cellulase in cellulose hydrolysis

In Jung Kim, Ki Hyun Nam, Eun Ju Yun, Sooah Kim, Hak Jin Youn, Hee Jin Lee, In Geol Choi, Kyoung Heon Kim

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Auxiliary activity family 9 (AA9, formerly known as glycoside hydrolase family 61 or polysaccharide monooxygenase) is a group of fungal proteins that were recently found to have a significant synergism with cellulase in cellulose hydrolysis via the oxidative cleavage of glycosidic bonds of cellulose chains. In this study, we report the active expression of a recombinant fungal AA9 from Chaetomium globosum (CgAA9) in a bacterial host, Escherichia coli, and the optimization of its synergistic activity in cellulose hydrolysis by using cellulase. The recombinant CgAA9 (0.9 mg/g cellulose) exhibited 1.7-fold synergism in the hydrolysis of Avicel when incubated with 0.9 filter paper units of Celluclast 1.5 L/g cellulose. The first study of the active expression of AA9 using a bacterial host and its synergistic optimization could be useful for the industrial application of AA9 for the saccharification of lignocellulose.

Original languageEnglish
Pages (from-to)8537-8547
Number of pages11
JournalApplied Microbiology and Biotechnology
Volume99
Issue number20
DOIs
Publication statusPublished - 2015 Oct 22

Keywords

  • AA9
  • Cellulase
  • Cellulose hydrolysis
  • Chaetomium globosum
  • GH61
  • Synergism

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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