A highly thermostable β-(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 β-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 C and pH 5.0. In addition, this enzymeo was extremely thermostable, showing a half-life of 113 h at 85 C. These results indicate thato rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.
Bibliographical noteFunding Information:
This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Korean government (MEST) (No. 2014R1A2A2A05002744).
© 2017 by The Korean Society for Microbiology and Biotechnology.
All Science Journal Classification (ASJC) codes
- Applied Microbiology and Biotechnology