Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium 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 degrees C. The enzyme was greatly suppressed by Ca(2+), Cu(2+), Co(2+), and Fe(2+) ions but not by Mg(2+) and Mn(2+). 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-beta-1,4-xylanase with some properties that are distinct from those of GH family 10.
Oh
Hyun-Woo
HW
Biological Resources Center, KRIBB, Daejeon, South Korea.
Heo
Sun-Yeon
SY
Kim
Do Young
DY
Park
Doo-Sang
DS
Bae
Kyung Sook
KS
Park
Ho-Yong
HY
D000192:Actinomycetales / Q000201:enzymology* / Q000235:genetics* / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004795:Enzyme Stability; D006135:Gryllidae / Q000382:microbiology* / Q000502:physiology; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013379:Substrate Specificity; D013559:Symbiosis
D043364:Endo-1,4-beta Xylanases