Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Novel Alkali-Tolerant GH10 Endo-${\beta}$-1,4-Xylanase with Broad Substrate Specificity from Microbacterium trichothecenolyticum HY-17, a Gut Bacterium of the Mole Cricket Gryllotalpa orientalis

  • Kim, Do Young (Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Shin, Dong-Ha (Insect Biotech Co. Ltd.) ;
  • Jung, Sora (Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Kim, Hyangmi (Microbial Resource Center, KRIBB) ;
  • Lee, Jong Suk (Gyeonggi Bio-Center, Gyeonggi Institute of Science & Technology Promotion) ;
  • Cho, Han-Young (Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Bae, Kyung Sook (Microbial Resource Center, KRIBB) ;
  • Sung, Chang-Keun (Department of Food Science and Technology, Chungnam National University) ;
  • Rhee, Young Ha (Department of Microbiology and Molecular Biology, Chungnam National University) ;
  • Son, Kwang-Hee (Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Park, Ho-Yong (Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
  • Received : 2014.05.15
  • Accepted : 2014.05.24
  • Published : 2014.07.28
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Abstract

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 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylosebased 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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References

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