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J Microbiol Biotechnol. 2017 Feb 28;27(2):271-276. doi: 10.4014/jmb.1609.09022.

Enzymatic Characteristics of a Highly Thermostable β-(1-4)-Glucanase from Fervidobacterium islandicum AW-1 (KCTC 4680).

Author information

1
Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University, Yongin 17104, Republic of Korea.
2
Korea Food Research Institute, Seongnam 13539, Republic of Korea.
3
Research Division for Biotechnology, Korea Atomic Energy Research Institute, Jeongeup 56212, Republic of Korea.
4
School of Applied Biosciences, Kyungpook National University, Daegu 41566, Republic of Korea.
5
Department of Food Science and Biotechnology, Gachon University, Seongnam 13120, Republic of Korea.

Abstract

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 enzyme was extremely thermostable, showing a half-life of 113 h at 85°C. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.

KEYWORDS:

Cellulase; Fervidobacterium islandicum; extremozyme; thermophilic enzyme; β-(1-4)-glucanase; β-glucan

PMID:
27780955
DOI:
10.4014/jmb.1609.09022
[Indexed for MEDLINE]
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