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Title 

Novel alkali-tolerant GH10 endo-β-1,4-xylanase with broad substrate specificity from Microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis

Authors 

Do Young KimD H ShinSora JungHyangmi KimJ S LeeHan-Young ChoKyung Sook BaeC K SungY H RheeKwang- Hee SonHo Yong Park

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2014

Citation 

Journal of Microbiology and Biotechnology, vol. 24, no. 7, pp. 943-953

Keywords 

4-xylanaseEndo-β-1GH10 enzymeGut bacteriumMicrobacterium trichothecenolyticum HY-17Mole cricket

Abstract 

The XylH gene (1167-bp) encoding a novel hemicellulase (41,584 Da) was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis. The enzyme consisted of a single catalytic domain, which is 74% identical to that ofof an endo-β-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-β-1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multi-functional enzyme possessing endo-beta-1,4-xylanase activity together with beta-1,3/beta-1,4-glucanase activity, which exhibited its highest xylanolytic activity at pH 9.0 and 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylose-based polysaccharides to the XylH were assessed to be as follows: oat spelts xylan > beechwood xylan > birchwood xylan > wheat arabinoxylan. rXylH was also able to readily cleave p-nitrophenyl (pNP) cellobioside and pNP-xylopyranoside but did not hydrolyze other pNP-sugar derivatives, xylobiose, or hexose-based materials. Enzymatic hydrolysis of birchwood xylan resulted in the product composition of xylobiose (71.2%) and xylotriose (28.8%) as end products.

ISSN 

1017-7825

Link 

http://dx.doi.org/10.4014/jmb.1405.05032

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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