Enzymatic Characteristics of a Highly Thermostable beta-(1-4)-Glucanase from Fervidobacterium islandicum AW-1 (KCTC 4680)
2017
Jeong, W.S., Kyung Hee University, Yongin, Republic of Korea | Seo, D.H., Kyung Hee University, Yongin, Republic of Korea | Jung, J.H., Kyung Hee University, Yongin, Republic of Korea | Jung, D.H., Kyung Hee University, Yongin, Republic of Korea | Lee, D.W., Kyungpook National University, Daegu, Republic of Korea | Park, Y.S., Gachon University, Seongnam, Republic of Korea | Park, C.S., Kyung Hee University, Yongin, Republic of Korea
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 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 90o C and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at 85o C. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.
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