期刊
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
卷 27, 期 2, 页码 271-276出版社
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.1609.09022
关键词
Cellulase; extremozyme; Fervidobacterium islandicum; beta-glucan; beta-(1-4)-glucanase; thermophilic enzyme
资金
- National Research Foundation of Korea (NRF) grant - Korean government (MEST) [2014R1A2A2A05002744]
- National Research Foundation of Korea [2014R1A2A2A05002744] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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