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KMID : 0545120170270020271
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Journal of Microbiology and Biotechnology
2017 Volume.27 No. 2 p.271 ~ p.276
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Enzymatic Characteristics of a Highly Thermostable β-(1-4)-Glucanase from Fervidobacterium islandicum AW-1 (KCTC 4680)
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Jeong Woo-Soo
Seo Dong-Ho
Jung Jong-Hyun
Jung Dong-Hyun
Lee Dong-Woo
Park Young-Seo
Park Cheon-Seok
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Abstract
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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 90oC and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at 85oC. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.
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KEYWORD
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Cellulase, Fervidobacterium islandicum, β-glucan, β-(1-4)-glucanase, thermophilic enzyme
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