Distinct Actions by Paenibacillus sp Strain E18 alpha-L-Arabinofuranosidases and Xylanase in Xylan Degradation

文献类型： 外文期刊

第一作者： Shi, Pengjun

作者： Shi, Pengjun;Chen, Xiaoyan;Meng, Kun;Huang, Huoqing;Bai, Yingguo;Luo, Huiying;Yang, Peilong;Yao, Bin

作者机构：

期刊名称：APPLIED AND ENVIRONMENTAL MICROBIOLOGY （ 影响因子：4.792； 五年影响因子：5.26 ）

ISSN： 0099-2240

年卷期： 2013 年 79 卷 6 期

页码：

收录情况： SCI

摘要： We cloned a Paenibacillus sp. strain E18 5.3-kb xylanolytic gene cluster that contains three open reading frames encoding two family 43 alpha-L-arabinofuranosidases (Abf43A and Abf43B) and one family 10 xylanase (XynBE18). The deduced amino acid sequences of Abf43A and Abf43B were at most 68% and 63% identical to those of two putative family 43 proteins from Clostridium sp. strain DL-VIII (EHI98634.1 and EHI98635.1), respectively, but were only 11% identical to each other. Recombinant Abf43A and Abf43B had similar activities at 45 degrees C and pH 6.0 but varied in thermostabilities and substrate specificities. Abf43B was active against only 4-nitrophenyl alpha-L-arabinofuranoside, whereas Abf43A acted on 4-nitrophenyl alpha-L-arabinofuranoside, wheat arabinoxylan, 4-nitrophenyl alpha-D-xylopyranoside, and sugar beet arabinan. The sequential and combined effects on xylan degradation by XynBE18, Abf43A, and Abf43B were characterized. For beechwood, birchwood, and oat spelt xylans as the substrates, synergistic effects were found when XynBE18 and Abf43A or Abf43B were incubated together and when the substrates were first incubated with Abf43A or Abf43B and then with XynBE18. Further high-performance liquid chromatography (HPLC) analysis showed that the amounts of xylobiose and xylose increased sharply in the aforementioned reactions. For water-soluble wheat arabinoxylan as the substrate, Abf43A not only released arabinose but also had a synergistic effect with XynBE18. Synergy may arise as the result of removal of arabinose residues from xylans by alpha-L-arabinofuranosidases, which eliminates steric hindrance caused by the arabinose side chains and which allows xylanases to then degrade the xylan backbone, producing short xylooligosaccharides.

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