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Optimization of synergism of a recombinant auxiliary activity 9 from Chaetomium globosum with cellulase in cellulose hydrolysis
- 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.
- Subjects :
- Glycoside Hydrolases
Cellulase
Chaetomium
Polysaccharide
Applied Microbiology and Biotechnology
chemistry.chemical_compound
Hydrolysis
AA9
GH61
Escherichia coli
Glycoside hydrolase
Cellulose
Biotechnologically Relevant Enzymes and Proteins
chemistry.chemical_classification
Fungal protein
biology
Chaetomium globosum
Synergism
General Medicine
biology.organism_classification
Recombinant Proteins
Cellulose hydrolysis
chemistry
Biochemistry
biology.protein
Biotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 14320614 and 01757598
- Volume :
- 99
- Database :
- OpenAIRE
- Journal :
- Applied Microbiology and Biotechnology
- Accession number :
- edsair.doi.dedup.....e99335e4dbc21b354e53b83bd280f230