Abstract
An exo-symbiotic bacterium capable of hydrolyzing xylan was isolated from the gut of the mole cricket, Gryllotalpa orientalis, and identified as Cellulosimicrobium sp. HY-12. The xylanase (XylACspHY-12) of this organism bound tightly to both DEAE and mono Q resins, and its molecular mass (M r) was about 39.0 kDa. The highest xylanase activity was observed at pH 6.0 and 60°C. The enzyme was greatly suppressed by Ca2+, Cu2+, Co2+, and Fe2+ ions but not by Mg2+ and Mn2+. Although XylACspHY-12 was capable of hydrolyzing various types of xylosic compounds, it could not decompose carboxymethyl cellulose or xylobiose. The xylA CspHY-12 gene consisted of an 1,188 bp open reading frame that encoded a polypeptide of 395 amino acids with a deduced molecular mass of 42,925 Da. The domain structure of XylACspHY-12 was most similar to those of the glycoside hydrolase (GH) family 10 endoxylanases. However its sequence identity with any of the enzymes in this family was below 52%. The results of this study suggest that the XylACspHY-12 is a new cellulase-free endo-β-1,4-xylanase with some properties that are distinct from those of GH family 10.
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Acknowledgements
This work was supported by a grant from KRIBB Research Initiative Program (KGM2300613) and the 21C Frontier Microbial Genomics and Applications Center Program (MGM0900726) of the Korean Ministry of Science and Technology.
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Oh, HW., Heo, SY., Kim, D.Y. et al. Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12. Antonie van Leeuwenhoek 93, 437–442 (2008). https://doi.org/10.1007/s10482-007-9210-2
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DOI: https://doi.org/10.1007/s10482-007-9210-2