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

Authors :
In Geol Choi
Eun Ju Yun
Hak Jin Youn
Kyoung Heon Kim
Sooah Kim
Hee Jin Lee
Ki Hyun Nam
In Jung Kim
Source :
Applied Microbiology and Biotechnology
Publication Year :
2015
Publisher :
Springer Berlin Heidelberg, 2015.

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. Electronic supplementary material The online version of this article (doi:10.1007/s00253-015-6592-3) contains supplementary material, which is available to authorized users.

Details

Language :
English
ISSN :
14320614 and 01757598
Volume :
99
Database :
OpenAIRE
Journal :
Applied Microbiology and Biotechnology
Accession number :
edsair.doi.dedup.....e99335e4dbc21b354e53b83bd280f230