Improved Expression and Characterization of a Multidomain Xylanase from Thermoanaerobacterium aotearoense SCUT27 in Bacillus subtilis

Xiongliang Huang, Zhe Li, Chenyu Du, Jufang Wang, Shuang Li

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A xylanase gene was cloned and characterized from Thermoanerobacterium aotearoense SCUT27, which was attested to consist of a signal peptide, one glycoside hydrolase family 10 domain, four carbohydrate binding modules, and three surface layer homology domains. The change of expression host from Escherichia coli to Bacillus subtilis resulted in a 4.1-fold increase of specific activity for the truncated XynAΔSLH. Five different versions of secretion signals in B. subtilis indicated that it was preferably routed via a Sec-dependent pathway. Purified XynAΔSLH showed a high activity of 379.8 U/mg on beechwood xylan. XynAΔSLH was optimally active at 80 °C, pH 6.5. Thin layer chromatography results showed that xylobiose and the presumed methylglucuronoxylotriose (MeGlcAXyl3) were the main products liberated from beechwood xylan catalyzed by the recombinant xylanase. All of the results suggest that XynAΔSLH is a suitable candidate for generating xylooligosaccharides from cellulosic materials for industrial uses.

LanguageEnglish
Pages6430-6439
Number of pages10
JournalJournal of Agricultural and Food Chemistry
Volume63
Issue number28
DOIs
Publication statusPublished - 22 Jul 2015

Fingerprint

Thermoanaerobacterium aotearoense
Thermoanaerobacterium
Xylans
xylan
xylanases
Bacilli
Bacillus subtilis
cellulosic materials
xylooligosaccharides
Thin layer chromatography
carbohydrate binding
Glycoside Hydrolases
Thin Layer Chromatography
Protein Sorting Signals
hydrolases
signal peptide
sequence homology
thin layer chromatography
Escherichia coli
glycosides

Cite this

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title = "Improved Expression and Characterization of a Multidomain Xylanase from Thermoanaerobacterium aotearoense SCUT27 in Bacillus subtilis",
abstract = "A xylanase gene was cloned and characterized from Thermoanerobacterium aotearoense SCUT27, which was attested to consist of a signal peptide, one glycoside hydrolase family 10 domain, four carbohydrate binding modules, and three surface layer homology domains. The change of expression host from Escherichia coli to Bacillus subtilis resulted in a 4.1-fold increase of specific activity for the truncated XynAΔSLH. Five different versions of secretion signals in B. subtilis indicated that it was preferably routed via a Sec-dependent pathway. Purified XynAΔSLH showed a high activity of 379.8 U/mg on beechwood xylan. XynAΔSLH was optimally active at 80 °C, pH 6.5. Thin layer chromatography results showed that xylobiose and the presumed methylglucuronoxylotriose (MeGlcAXyl3) were the main products liberated from beechwood xylan catalyzed by the recombinant xylanase. All of the results suggest that XynAΔSLH is a suitable candidate for generating xylooligosaccharides from cellulosic materials for industrial uses.",
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Improved Expression and Characterization of a Multidomain Xylanase from Thermoanaerobacterium aotearoense SCUT27 in Bacillus subtilis. / Huang, Xiongliang; Li, Zhe; Du, Chenyu; Wang, Jufang; Li, Shuang.

In: Journal of Agricultural and Food Chemistry, Vol. 63, No. 28, 22.07.2015, p. 6430-6439.

Research output: Contribution to journalArticle

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