Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of <Emphasis Type="Italic">Gryllotalpa orientalis</Emphasis>, <Emphasis Type="Italic">Cellulosimicrobium</Emphasis> sp. HY-12

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 (XylA _CspHY-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 XylA _CspHY-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 XylA _CspHY-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 XylA _CspHY-12 is a new cellulase-free endo-β-1,4-xylanase with some properties that are distinct from those of GH family 10.