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

doi:10.4014/jmb.1609.09022

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

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

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

Original language	English
Pages (from-to)	271-276
Number of pages	6
Journal	Journal of microbiology and biotechnology
Volume	27
Issue number	2
DOIs	https://doi.org/10.4014/jmb.1609.09022
Publication status	Published - 2017 Feb

Bibliographical note

Publisher Copyright:
© 2017 by The Korean Society for Microbiology and Biotechnology.

All Science Journal Classification (ASJC) codes

Biotechnology
Applied Microbiology and Biotechnology

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10.4014/jmb.1609.09022

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

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 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.",

keywords = "Cellulase, Extremozyme, Fervidobacterium islandicum, Thermophilic enzyme, β-(1-4)-glucanase, β-glucan",

author = "Jeong, {Woo Soo} and Seo, {Dong Ho} and Jung, {Jong Hyun} and Jung, {Dong Hyun} and Lee, {Dong Woo} and Park, {Young Seo} and Park, {Cheon Seok}",

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year = "2017",

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doi = "10.4014/jmb.1609.09022",

language = "English",

volume = "27",

pages = "271--276",

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T1 - Enzymatic characteristics of a highly thermostable β-(1-4)-glucanase from fervidobacterium islandicum aw-1 (KCTC 4680)

AU - Jeong, Woo Soo

AU - Seo, Dong Ho

AU - Jung, Jong Hyun

AU - Jung, Dong Hyun

AU - Lee, Dong Woo

AU - Park, Young Seo

AU - Park, Cheon Seok

PY - 2017/2

Y1 - 2017/2

N2 - 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.

AB - 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.

KW - Cellulase

KW - Extremozyme

KW - Fervidobacterium islandicum

KW - Thermophilic enzyme

KW - β-(1-4)-glucanase

KW - β-glucan

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

Abstract

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