Journal
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume 24, Issue 7, Pages 943-953Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.1405.05032
Keywords
Endo-beta-1,4-xylanase; GH10 enzyme; Microbacterium trichothecenolyticum HY-17; mole cricket; gut bacterium
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Funding
- KRIBB Research Initiative Program of the Ministry of Science, ICT & Future Planning [KGM2131413, KCS3071413]
- Ministry of Agriculture, Food and Rural Affairs, Republic of Korea [AGM0111213]
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The XylH gene (1,167-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 of an endo-beta-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-beta-1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multifunctional 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 60 degrees C, 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.
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