Discovery and characterization of endo-xylanase and beta-xylosidase from a highly xylanolytic bacterium in the hindgut of Holotrichia parallela larvae

文献类型： 外文期刊

第一作者： Xu, Jing

作者： Xu, Jing;Zhang, Hongyu;Sheng, Ping;Xu, Jing;Zhang, Hongyu;Saccone, Giuseppe;Li, Kebin

作者机构：

关键词： Endo-xylanase;beta-Xylosidase;Synergy;Xylose tolerance;Holotrichia parallela

期刊名称：JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC （ 影响因子：2.269； 五年影响因子：2.328 ）

ISSN： 1381-1177

年卷期： 2014 年 105 卷

页码：

收录情况： SCI

摘要： A highly xylanolytic bacterium, Sphingobacterium sp. HP455, was isolated from the hindgut of soildwelling Holotrichia parallela larvae. The endo-xylanase (Xyn455) gene of the glycoside hydrolase (GH) family 10 and p-xylosidase (Xy1455) gene of the GH43 family were cloned and expressed in vitro from this highly xylanolytic bacterium. Both the Xyn455 and Xy1455 enzymes acted on a broad range of hemicelluloses. Xyn455 cleaved xylan to liberate xylooligosaccharides (XOS), and the XOS were subsequently cleaved into xylose through the action of Xy1455. This synergistic action significantly increased the xylan hydrolysis to 62.8%, which is higher than the sum of hydrolysis achieved by the enzymes individually (26.65%). Furthermore, Xy1455 is a bifunctional enzyme with both beta-D-xylosidase and alpha-L-arabinofuranosidase activities. Xy1455 also exhibits high xylose tolerance and a broad pH stability. The pH-dependent half-lives of Xy1455 range from 8.77 h to 43.52 h after pre-incubation for 1 h at 4 degrees C in buffers ranging from pH 3.0 to 9.0. These results suggest that both recombinant Xyn455 and Xy1455 and the bacterium are potential candidates to be used in commercial biomass conversion. (C) 2014 Elsevier B.V. All rights reserved.

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