Enzymatic characteristics of a highly thermostable β-(1-4)-glucanase from fervidobacterium islandicum aw-1 (KCTC 4680)

Woo Soo Jeong, Dong Ho Seo, Jong Hyun Jung, Dong Hyun Jung, Dong Woo Lee, Young Seo Park, Cheon Seok Park

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2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)271-276
Number of pages6
JournalJournal of microbiology and biotechnology
Issue number2
Publication statusPublished - 2017 Feb


All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

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