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首页> 外文期刊>Renewable Agriculture and Food Systems >Characterization of the arabinoxylan-degrading machinery of the thermophilic bacterium Herbinix hemicellulosilytica-Six new xylanases, three arabinofuranosidases and one xylosidase
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Characterization of the arabinoxylan-degrading machinery of the thermophilic bacterium Herbinix hemicellulosilytica-Six new xylanases, three arabinofuranosidases and one xylosidase

机译：嗜热细菌植物中草叶素含量 - 六个新木聚糖酶，三种阿拉伯呋喃酶和一种木糖苷酶的阿拉伯辛Xylan降解机械的特征

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摘要

Herbinix hemicellulosilytica is a newly isolated, gram-positive, anaerobic bacterium with extensive hemicellulose-degrading capabilities obtained from a thermophilic biogas reactor. In order to exploit its potential as a source for new industrial arabinoxylan-degrading enzymes, six new thermophilic xylanases, four from glycoside hydrolase family 10 (GH10) and two from GH11, three arabinofuranosidases (1x GH43, 2x GH51) and one beta-xylosidase (GH43) were selected. The recombinantly produced enzymes were purified and characterized. All enzymes were active on different xylan-based polysaccharides and most of them showed temperature-vs-activity profiles with maxima around 55-65 degrees C. HPAEC-PAD analysis of the hydrolysates of wheat arabinoxylan and of various purified xylooligosaccharides (XOS) and arabinoxylooligosaccharides (AXOS) was used to investigate their substrate and product specificities: among the GH10 xylanases, XynB showed a different product pattern when hydrolysing AXOS compared to XynA, XynC, and XynD. None of the GH11 xylanases was able to degrade any of the tested AXOS. All three arabinofuranosidases, ArfA, ArfB and ArfC, were classified as type AXH-m, d enzymes. None of the arabinofuranosidases was able to degrade the double-arabinosylated xylooligosaccharides XA(2+3)XX. beta-Xylosidase XylA (GH43) was able to degrade unsubstituted XOS, but showed limited activity to degrade AXOS.
机译：Herbinix Hemicellulosilytica是一种新的革兰氏阳性的厌氧细菌，具有从嗜热沼气反应器获得的广泛的半纤维素降解能力。为了利用其作为新工业阿拉伯氧基 - 降解酶的源泉，六种新的嗜热木聚糖酶，来自糖苷水解酶10（GH10）的四种（GH10）和来自GH11，三种阿拉伯呋喃糖苷酶（1x GH43，2X GH51）和一个β-木质素酶（GH43）被选中。重组产生的酶被纯化并表征。所有酶在不同的基于木聚糖的多糖上活跃，并且它们中的大部分显示出温度-Vs-活性曲线，最大值为55-65摄氏度约55-65摄氏度。HPAEC焊盘分析小麦阿拉伯毒糖酸盐和各种纯化的木龙核苷酸（XOS）和阿拉伯毒珠酮糖（轴）用于研究其基材和产品特异性：在GH10木聚糖酶中，与XYNA，XYNC和XYND相比，Xynb在水解轴时显示出不同的产品图案。 GH11木聚糖酶没有均可降解任何测试的轴。所有三种阿拉伯呋喃糖苷酶，ARFA，ARFB和ARFC被分类为AXH-M，D酶类型。没有一种阿拉伯呋喃磷酸酶能够降解双阿拉伯糖基化的木质糖苷酸Xa（2 + 3）XX。 β-木糖苷酶Xyla（GH43）能够降解未取代的XO，但显示有限的活性以降解轴。

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