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Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12.
- Source :
-
Antonie van Leeuwenhoek [Antonie Van Leeuwenhoek] 2008 May; Vol. 93 (4), pp. 437-42. Date of Electronic Publication: 2007 Nov 20. - Publication Year :
- 2008
-
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 (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.
- Subjects :
- Actinomycetales physiology
Amino Acid Sequence
Animals
Endo-1,4-beta Xylanases genetics
Enzyme Stability
Gryllidae physiology
Molecular Sequence Data
Sequence Alignment
Substrate Specificity
Actinomycetales enzymology
Actinomycetales genetics
Endo-1,4-beta Xylanases chemistry
Endo-1,4-beta Xylanases metabolism
Gryllidae microbiology
Symbiosis
Subjects
Details
- Language :
- English
- ISSN :
- 0003-6072
- Volume :
- 93
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Antonie van Leeuwenhoek
- Publication Type :
- Academic Journal
- Accession number :
- 18027102
- Full Text :
- https://doi.org/10.1007/s10482-007-9210-2