Optimization of synergism of a recombinant auxiliary activity 9 from Chaetomium globosum with cellulase in cellulose hydrolysis
- Authors
- Kim, In Jung; Nam, Ki Hyun; Yun, Eun Ju; Kim, Sooah; Youn, Hak Jin; Lee, Hee Jin; Choi, In-Geol; Kim, Kyoung Heon
- Issue Date
- Oct-2015
- Publisher
- SPRINGER
- Keywords
- AA9; GH61; Synergism; Cellulose hydrolysis; Cellulase; Chaetomium globosum
- Citation
- APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.99, no.20, pp.8537 - 8547
- Indexed
- SCIE
SCOPUS
- Journal Title
- APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 99
- Number
- 20
- Start Page
- 8537
- End Page
- 8547
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/92418
- DOI
- 10.1007/s00253-015-6592-3
- ISSN
- 0175-7598
- 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.
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