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PMID:20730475
| Citation |
Zhang, G, Mao, L, Zhao, Y, Xue, Y and Ma, Y (2010) Characterization of a thermostable xylanase from an alkaliphilic Bacillus sp. Biotechnol. Lett. 32:1915-20 |
|---|---|
| Abstract |
A xylanase gene (xyn10) from alkaliphilic Bacillus sp. N16-5 was cloned and expressed in Pichia pastoris. The deduced amino acid sequence has 85% identity with xylanase xyn10A from B. halodurans and contains two potential N-glycosylation sites. The glycosylated Xyn10 with MW 48 kDa can hydrolyze birchwood and oatspelt xylan. The enzyme had optimum activity at pH 7 and 70°C, with the specific activity of 92.5U/mg. The Xyn10 retained over 90% residual activity at 60°C for 30 min but lost all activity at 80°C over 15 min. Most tested ions showed no or slight inhibition effects on enzyme activity. |
| Links |
PubMed Online version:10.1007/s10529-010-0372-z |
| Keywords |
Bacillus/enzymology; Bacillus/genetics; Bacillus/metabolism; Cloning, Molecular; DNA, Bacterial/chemistry; DNA, Bacterial/genetics; Enzyme Stability; Gene Expression; Glycosylation; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Pichia/genetics; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Substrate Specificity; Temperature; Time Factors; Xylans/metabolism; Xylosidases/chemistry; Xylosidases/genetics; Xylosidases/isolation & purification; Xylosidases/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004553: hydrolase activity, hydrolyzing O-glycosyl compounds |
ECO:0000314: |
F |
The recombinant Xyn10 can hydrolyze xylan from oatspelt and birchwood, but cannot degrade methyl cellulose, citrus fruits pectin, maize starch, locust bean gum, or maize amylopectin (Table 3). Thus, Xyn10 is a specific xylanase. |
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Notes
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