Enzymatic Characteristics of a Highly Thermostable beta-(1-4)-Glucanase from Fervidobacterium islandicum AW-1 (KCTC 4680)
- Authors
- Jeong, Woo Soo; Seo, Dong Ho; Jung, Jong Hyun; Jung, Dong Hyun; Lee, Dong-Woo; Park, Young-Seo; Park, Cheon-Seok
- Issue Date
- Feb-2017
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Cellulase; extremozyme; Fervidobacterium islandicum; beta-glucan; beta-(1-4)-glucanase; thermophilic enzyme
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.27, no.2, pp.271 - 276
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 27
- Number
- 2
- Start Page
- 271
- End Page
- 276
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/6417
- DOI
- 10.4014/jmb.1609.09022
- ISSN
- 1017-7825
- Abstract
- A highly thermostable beta-(1-4)-glucanase (NA23_08975) gene (fig) from Fervidobacterium islandicum AW-1, a native-feather degrading thermophilic eubacterium, was cloned and expressed in Escherichia coli. The recombinant FiG (rFiG) protein showed strong activity toward beta-D-glucan from barley (367.0 IU/mg), galactomannan (174.0 IU/mg), and 4-nitrophenyl- cellobioside (66.1 IU/mg), but relatively weak activity was observed with hydroxyethyl cellulose (5.3 IU/mg), carboxymethyl cellulose (2.4 IU/mg), and xylan from oat spelt (1.4 IU/mg). rFiG exhibited optimal activity at 90 degrees C and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at 85 degrees C. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.
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