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Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-β-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus
- Title
- Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-β-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus
- Authors
- Song J.M.; Hong S.K.; An Y.J.; Kang M.H.; Hong K.H.; Lee Y.-H.; Cha S.-S.
- Ewha Authors
- 차선신
- SCOPUS Author ID
- 차선신
- Issue Date
- 2017
- Journal Title
- Journal of Agricultural and Food Chemistry
- ISSN
- 0021-8561
- Citation
- Journal of Agricultural and Food Chemistry vol. 65, no. 8, pp. 1630 - 1640
- Keywords
- biochemical and structural features; biofuel production from seaweeds; cold-active cellulase; Cryptopygus antarcticus; endo-β-1,4-glucanase; horizontal gene transfer
- Publisher
- American Chemical Society
- Indexed
- SCIE; SCOPUS
- Document Type
- Article
- Abstract
- The CaCel gene from Antarctic springtail Cryptopygus antarcticus codes for a cellulase belonging to the glycosyl hydrolase family 45 (GHF45). Phylogenetic, biochemical, and structural analyses revealed that the CaCel gene product (CaCel) is closely related to fungal GHF45 endo-β-1,4-glucanases. The organization of five introns within the open reading frame of the CaCel gene indicates its endogenous origin in the genome of the species, which suggests the horizontal transfer of the gene from fungi to the springtail. CaCel exhibited optimal activity at pH 3.5, retained 80% of its activity at 0-10 °C, and maintained a half-life of 4 h at 70 °C. Based on the structural comparison between CaCel and a fungal homologue, we deduced the structural basis for the unusual characteristics of CaCel. Under acidic conditions at 50 °C, CaCel was effective to digest the green algae (Ulva pertusa), suggesting that it could be exploited for biofuel production from seaweeds. © 2017 American Chemical Society.
- DOI
- 10.1021/acs.jafc.6b05037
- Appears in Collections:
- 자연과학대학 > 화학·나노과학전공 > Journal papers
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