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

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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
Author(s)
Do Young Kim; D H Shin; Sora Jung; Hyangmi Kim; J S Lee; Han Young Cho; Kyung Sook Bae; C K Sung; Y H Rhee; Kwang- Hee SonHo Yong Park
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 24, no. 7, pp. 943-953
Publication Year
2014
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.
Keyword
4-xylanaseEndo-β-1GH10 enzymeGut bacteriumMicrobacterium trichothecenolyticum HY-17Mole cricket
ISSN
1017-7825
Publisher
South Korea
DOI
http://dx.doi.org/10.4014/jmb.1405.05032
Type
Article
Appears in Collections:
Division of Biomaterials Research > Industrial Bio-materials Research Center > 1. Journal Articles
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