Journal of biotechnology, 2000-02, Vol.78 (1), p.83-86
2000
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Details
- Autor(en) / Beteiligte
- Titel
- Overproduction and characterization of seleno-methionine xylanase T-6
- Ist Teil von
- Journal of biotechnology, 2000-02, Vol.78 (1), p.83-86
- Ort / Verlag
- Lausanne: Elsevier B.V
- Erscheinungsjahr
- 2000
- Quelle
- Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
- Beschreibungen/Notizen
- The extracellular xylanase from Bacillus stearothermophilus T-6 is a thermostable alkaline tolerant enzyme that was found to bleach pulp optimally at pH 9 and 65°C, and was successfully used in a large-scale biobleaching mill trial. In an attempt to obtain a heavy atom derivative suitable for complete X-ray analysis, xylanase T-6 was labeled biosynthetically with seleno-methionine, resulting in a ‘built-in’ array of atoms with specific X-ray anomalous scattering signal. Optimization of growth conditions resulted in over 0.8 g of homogenous seleno-methionine xylanase T-6 per liter culture. The seleno-methionine enzyme was shown to be fully active and produced single crystals suitable for complete multiple wavelength anomalous diffraction (MAD) structural analysis.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0168-1656eISSN: 1873-4863DOI: 10.1016/S0168-1656(99)00226-6Titel-ID: cdi_proquest_miscellaneous_70972404
- Format
- –
- Schlagworte
- Bacillus stearothermophilus, Biological and medical sciences, Biotechnology, Biotechnology - methods, Crystallography, X-Ray, Escherichia coli, Fundamental and applied biological sciences. Psychology, Genetic engineering, Genetic technics, Geobacillus stearothermophilus - enzymology, Methods. Procedures. Technologies, Modification of gene expression level, Overproduction, Seleno-methionine, Selenomethionine - metabolism, Structure-Activity Relationship, Structure-function, X-ray, Xylan Endo-1,3-beta-Xylosidase, Xylanase, Xylosidases - biosynthesis, Xylosidases - chemistry