Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Enzymatic Characteristics of a Highly Thermostable β-(1-4)-Glucanase from Fervidobacterium islandicum AW-1 (KCTC 4680)

  • Jeong, Woo Soo (Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University) ;
  • Seo, Dong Ho (Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University) ;
  • Jung, Jong Hyun (Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University) ;
  • Jung, Dong Hyun (Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University) ;
  • Lee, Dong-Woo (School of Applied Biosciences, Kyungpook National University) ;
  • Park, Young-Seo (Department of Food Science and Biotechnology, Gachon University) ;
  • Park, Cheon-Seok (Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University)
  • Received : 2016.09.19
  • Accepted : 2016.10.14
  • Published : 2017.02.28
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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 ${\beta}-{\small{D}}-glucan$ 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 $90^{\circ}C$ and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at $85^{\circ}C$. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.

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